Frederick W. Dahlquist - Publications

Molecular, Cellular, and Developmental Biology University of California, Santa Barbara, Santa Barbara, CA, United States 
protein structure and function, nuclear magnetic resonance

198 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2019 Bartelli NL, Sun S, Gucinski GC, Zhou H, Song K, Hayes CS, Dahlquist FW. The Cytoplasm-Entry Domain of Antibacterial CdiA Is a Dynamic α-Helical Bundle with Disulfide-Dependent Structural Features. Journal of Molecular Biology. PMID 31181288 DOI: 10.1016/j.jmb.2019.05.049  0.72
2018 Ding X, He Q, Shen F, Dahlquist FW, Wang X. The Regulatory Role of an Interdomain Linker in the Bacterial Chemotaxis Histidine Kinase CheA. Journal of Bacteriology. PMID 29483161 DOI: 10.1128/JB.00052-18  0.48
2015 Pavlova A, Cheng CY, Kinnebrew M, Lew J, Dahlquist FW, Han S. Protein structural and surface water rearrangement constitute major events in the earliest aggregation stages of tau. Proceedings of the National Academy of Sciences of the United States of America. PMID 26712030 DOI: 10.1073/pnas.1504415113  1
2015 Yan H, Chuang C, Zhugayevych A, Tretiak S, Dahlquist FW, Bazan GC. Inter-aromatic distances in Geobacter sulfurreducens pili relevant to biofilm charge transport. Advanced Materials (Deerfield Beach, Fla.). 27: 1908-11. PMID 25604785 DOI: 10.1002/adma.201404167  1
2015 Maeno A, Sindhikara D, Hirata F, Otten R, Dahlquist FW, Yokoyama S, Akasaka K, Mulder FA, Kitahara R. Cavity as a source of conformational fluctuation and high-energy state: high-pressure NMR study of a cavity-enlarged mutant of T4 lysozyme. Biophysical Journal. 108: 133-45. PMID 25564860 DOI: 10.1016/j.bpj.2014.11.012  1
2015 Kirchhofer ND, Rasmussen MA, Dahlquist FW, Minteer SD, Bazan GC. The photobioelectrochemical activity of thylakoid bioanodes is increased via photocurrent generation and improved contacts by membrane-intercalating conjugated oligoelectrolytes Energy and Environmental Science. 8: 2698-2706. DOI: 10.1039/c5ee01707f  1
2014 Kirchhofer ND, Chen X, Marsili E, Sumner JJ, Dahlquist FW, Bazan GC. The conjugated oligoelectrolyte DSSN+ enables exceptional coulombic efficiency via direct electron transfer for anode-respiring Shewanella oneidensis MR-1-a mechanistic study. Physical Chemistry Chemical Physics : Pccp. 16: 20436-43. PMID 25171764 DOI: 10.1039/c4cp03197k  1
2014 Wang X, Vallurupalli P, Vu A, Lee K, Sun S, Bai WJ, Wu C, Zhou H, Shea JE, Kay LE, Dahlquist FW. The linker between the dimerization and catalytic domains of the CheA histidine kinase propagates changes in structure and dynamics that are important for enzymatic activity. Biochemistry. 53: 855-61. PMID 24444349 DOI: 10.1021/bi4012379  1
2013 Ortega DR, Mo G, Lee K, Zhou H, Baudry J, Dahlquist FW, Zhulin IB. Conformational coupling between receptor and kinase binding sites through a conserved salt bridge in a signaling complex scaffold protein. Plos Computational Biology. 9: e1003337. PMID 24244143 DOI: 10.1371/journal.pcbi.1003337  1
2013 Matje DM, Krivacic CT, Dahlquist FW, Reich NO. Distal structural elements coordinate a conserved base flipping network. Biochemistry. 52: 1669-76. PMID 23409802 DOI: 10.1021/bi301284f  1
2013 Matje DM, Zhou H, Smith DA, Neely RK, Dryden DT, Jones AC, Dahlquist FW, Reich NO. Enzyme-promoted base flipping controls DNA methylation fidelity. Biochemistry. 52: 1677-85. PMID 23409782 DOI: 10.1021/bi3012912  1
2012 Wang X, Wu C, Vu A, Shea JE, Dahlquist FW. Computational and experimental analyses reveal the essential roles of interdomain linkers in the biological function of chemotaxis histidine kinase CheA. Journal of the American Chemical Society. 134: 16107-10. PMID 22992224 DOI: 10.1021/ja3056694  1
2012 Vartanian AS, Paz A, Fortgang EA, Abramson J, Dahlquist FW. Structure of flagellar motor proteins in complex allows for insights into motor structure and switching. The Journal of Biological Chemistry. 287: 35779-83. PMID 22896702 DOI: 10.1074/jbc.C112.378380  1
2012 Levenson R, Zhou H, Dahlquist FW. Structural insights into the interaction between the bacterial flagellar motor proteins FliF and FliG. Biochemistry. 51: 5052-60. PMID 22670715 DOI: 10.1021/bi3004582  1
2012 Wang X, Vu A, Lee K, Dahlquist FW. CheA-receptor interaction sites in bacterial chemotaxis. Journal of Molecular Biology. 422: 282-90. PMID 22659323 DOI: 10.1016/j.jmb.2012.05.023  1
2012 Mo G, Zhou H, Kawamura T, Dahlquist FW. Solution structure of a complex of the histidine autokinase CheA with its substrate CheY. Biochemistry. 51: 3786-98. PMID 22494339 DOI: 10.1021/bi300147m  1
2012 Vu A, Wang X, Zhou H, Dahlquist FW. The receptor-CheW binding interface in bacterial chemotaxis. Journal of Molecular Biology. 415: 759-67. PMID 22155081 DOI: 10.1016/j.jmb.2011.11.043  1
2011 Vu A, Hamel DJ, Zhou H, Dahlquist FW. The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima. Journal of Biomolecular Nmr. 51: 49-55. PMID 21947914 DOI: 10.1007/s10858-011-9540-2  1
2011 Bouvignies G, Vallurupalli P, Hansen DF, Correia BE, Lange O, Bah A, Vernon RM, Dahlquist FW, Baker D, Kay LE. Solution structure of a minor and transiently formed state of a T4 lysozyme mutant. Nature. 477: 111-4. PMID 21857680 DOI: 10.1038/nature10349  1
2011 Kawamura T, Vartanian AS, Zhou H, Dahlquist FW. The design involved in PapI and Lrp regulation of the pap operon. Journal of Molecular Biology. 409: 311-32. PMID 21338611 DOI: 10.1016/j.jmb.2011.01.058  1
2011 Matje DM, Coughlin DF, Connolly BA, Dahlquist FW, Reich NO. Determinants of precatalytic conformational transitions in the DNA cytosine methyltransferase M.HhaI. Biochemistry. 50: 1465-73. PMID 21229971 DOI: 10.1021/bi101446g  1
2010 Peterson DW, Ando DM, Taketa DA, Zhou H, Dahlquist FW, Lew J. No difference in kinetics of tau or histone phosphorylation by CDK5/p25 versus CDK5/p35 in vitro. Proceedings of the National Academy of Sciences of the United States of America. 107: 2884-9. PMID 20133653 DOI: 10.1073/pnas.0912718107  1
2009 Pavlova A, McCarney ER, Peterson DW, Dahlquist FW, Lew J, Han S. Site-specific dynamic nuclear polarization of hydration water as a generally applicable approach to monitor protein aggregation. Physical Chemistry Chemical Physics : Pccp. 11: 6833-9. PMID 19639158 DOI: 10.1039/b906101k  1
2009 Zhou H, Purdy MM, Dahlquist FW, Reich NO. The recognition pathway for the DNA cytosine methyltransferase M.HhaI. Biochemistry. 48: 7807-16. PMID 19580326 DOI: 10.1021/bi900502g  1
2009 Hao S, Hamel D, Zhou H, Dahlquist FW. Structural basis for the localization of the chemotaxis phosphatase CheZ by CheAS. Journal of Bacteriology. 191: 5842-4. PMID 19502407 DOI: 10.1128/JB.00323-09  1
2009 Dyer CM, Vartanian AS, Zhou H, Dahlquist FW. A molecular mechanism of bacterial flagellar motor switching. Journal of Molecular Biology. 388: 71-84. PMID 19358329 DOI: 10.1016/j.jmb.2009.02.004  1
2008 Peterson DW, Zhou H, Dahlquist FW, Lew J. A soluble oligomer of tau associated with fiber formation analyzed by NMR. Biochemistry. 47: 7393-404. PMID 18558718 DOI: 10.1021/bi702466a  1
2008 Cecconi C, Shank EA, Dahlquist FW, Marqusee S, Bustamante C. Protein-DNA chimeras for single molecule mechanical folding studies with the optical tweezers. European Biophysics Journal : Ebj. 37: 729-38. PMID 18183383 DOI: 10.1007/s00249-007-0247-y  1
2007 Caballero-Manrique E, Bray JK, Deutschman WA, Dahlquist FW, Guenza MG. A theory of protein dynamics to predict NMR relaxation. Biophysical Journal. 93: 4128-40. PMID 17766356 DOI: 10.1529/biophysj.107.111849  1
2007 Park MJ, Dahlquist FW, Doyle FJ. Simultaneous high gain and wide dynamic range in a model of bacterial chemotaxis. Iet Systems Biology. 1: 222-9. PMID 17708429 DOI: 10.1049/iet-syb:20070003  1
2007 Zhou H, Shatz W, Purdy MM, Fera N, Dahlquist FW, Reich NO. Long-range structural and dynamical changes induced by cofactor binding in DNA methyltransferase M.HhaI. Biochemistry. 46: 7261-8. PMID 17523600 DOI: 10.1021/bi602662e  1
2007 Peterson SN, Dahlquist FW, Reich NO. The role of high affinity non-specific DNA binding by Lrp in transcriptional regulation and DNA organization. Journal of Molecular Biology. 369: 1307-17. PMID 17498742 DOI: 10.1016/j.jmb.2007.04.023  1
2007 Lundström P, Vallurupalli P, Religa TL, Dahlquist FW, Kay LE. A single-quantum methyl 13C-relaxation dispersion experiment with improved sensitivity. Journal of Biomolecular Nmr. 38: 79-88. PMID 17464570 DOI: 10.1007/s10858-007-9149-7  1
2007 Cellitti J, Llinas M, Echols N, Shank EA, Gillespie B, Kwon E, Crowder SM, Dahlquist FW, Alber T, Marqusee S. Exploring subdomain cooperativity in T4 lysozyme I: structural and energetic studies of a circular permutant and protein fragment. Protein Science : a Publication of the Protein Society. 16: 842-51. PMID 17400926 DOI: 10.1110/ps.062628607  1
2007 Kawamura T, Le LU, Zhou H, Dahlquist FW. Solution structure of Escherichia coli PapI, a key regulator of the pap pili phase variation. Journal of Molecular Biology. 365: 1130-42. PMID 17109885 DOI: 10.1016/j.jmb.2006.10.066  1
2006 Dyer CM, Dahlquist FW. Switched or not?: the structure of unphosphorylated CheY bound to the N terminus of FliM. Journal of Bacteriology. 188: 7354-63. PMID 17050923 DOI: 10.1128/JB.00637-06  1
2006 Krushelnitsky A, Gogolev Y, Golbik R, Dahlquist F, Reichert D. Comparison of the internal dynamics of globular proteins in the microcrystalline and rehydrated lyophilized states. Biochimica Et Biophysica Acta. 1764: 1639-45. PMID 17027351 DOI: 10.1016/j.bbapap.2006.08.015  1
2006 Hamel DJ, Zhou H, Starich MR, Byrd RA, Dahlquist FW. Chemical-shift-perturbation mapping of the phosphotransfer and catalytic domain interaction in the histidine autokinase CheA from Thermotoga maritima. Biochemistry. 45: 9509-17. PMID 16878985 DOI: 10.1021/bi060798k  1
2006 Dahlquist FW. Slip sliding away: new insights into DNA-protein recognition. Nature Chemical Biology. 2: 353-4. PMID 16783338 DOI: 10.1038/nchembio0706-353  1
2005 Hamel DJ, Dahlquist FW. The contact interface of a 120 kD CheA-CheW complex by methyl TROSY interaction spectroscopy. Journal of the American Chemical Society. 127: 9676-7. PMID 15998058 DOI: 10.1021/ja052517m  1
2005 Quezada CM, Hamel DJ, Gradinaru C, Bilwes AM, Dahlquist FW, Crane BR, Simon MI. Structural and chemical requirements for histidine phosphorylation by the chemotaxis kinase CheA. The Journal of Biological Chemistry. 280: 30581-5. PMID 15994328 DOI: 10.1074/jbc.M505316200  1
2004 Dyer CM, Quillin ML, Campos A, Lu J, McEvoy MM, Hausrath AC, Westbrook EM, Matsumura P, Matthews BW, Dahlquist FW. Structure of the constitutively active double mutant CheYD13K Y106W alone and in complex with a FliM peptide. Journal of Molecular Biology. 342: 1325-35. PMID 15351654 DOI: 10.1016/j.jmb.2004.07.084  1
2004 Kingston RL, Hamel DJ, Gay LS, Dahlquist FW, Matthews BW. Structural basis for the attachment of a paramyxoviral polymerase to its template. Proceedings of the National Academy of Sciences of the United States of America. 101: 8301-6. PMID 15159535 DOI: 10.1073/pnas.0402690101  1
2003 Korzhnev DM, Orekhov VY, Dahlquist FW, Kay LE. Off-resonance R1rho relaxation outside of the fast exchange limit: an experimental study of a cavity mutant of T4 lysozyme. Journal of Biomolecular Nmr. 26: 39-48. PMID 12766401 DOI: 10.1023/A:1023039902737  1
2002 Griswold IJ, Dahlquist FW. The dynamic behavior of CheW from Thermotoga maritima in solution, as determined by nuclear magnetic resonance: implications for potential protein-protein interaction sites. Biophysical Chemistry. 101: 359-73. PMID 12488014 DOI: 10.1016/S0301-4622(02)00157-6  1
2002 Eldridge AM, Kang HS, Johnson E, Gunsalus R, Dahlquist FW. Effect of phosphorylation on the interdomain interaction of the response regulator, NarL. Biochemistry. 41: 15173-80. PMID 12484754 DOI: 10.1021/bi026254+  1
2002 Skrynnikov NR, Dahlquist FW, Kay LE. Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments. Journal of the American Chemical Society. 124: 12352-60. PMID 12371879 DOI: 10.1021/ja0207089  1
2002 Griswold IJ, Dahlquist FW. Bigger is better: megadalton protein NMR in solution. Nature Structural Biology. 9: 567-8. PMID 12145644 DOI: 10.1038/nsb0802-567  1
2002 Dahlquist FW. Amplification of signaling events in bacteria. Science's Stke : Signal Transduction Knowledge Environment. 2002: pe24. PMID 12011494 DOI: 10.1126/stke.2002.132.pe24  1
2002 Boukhvalova MS, Dahlquist FW, Stewart RC. CheW binding interactions with CheA and Tar. Importance for chemotaxis signaling in Escherichia coli. The Journal of Biological Chemistry. 277: 22251-9. PMID 11923283 DOI: 10.1074/jbc.M110908200  1
2002 Mulder FA, Hon B, Mittermaier A, Dahlquist FW, Kay LE. Slow internal dynamics in proteins: application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society. 124: 1443-51. PMID 11841314 DOI: 10.1021/ja0119806  1
2002 Griswold IJ, Zhou H, Matison M, Swanson RV, McIntosh LP, Simon MI, Dahlquist FW. The solution structure and interactions of CheW from Thermotoga maritima. Nature Structural Biology. 9: 121-5. PMID 11799399 DOI: 10.1038/nsb753  1
2001 Mulder FA, Mittermaier A, Hon B, Dahlquist FW, Kay LE. Studying excited states of proteins by NMR spectroscopy. Nature Structural Biology. 8: 932-5. PMID 11685237 DOI: 10.1038/nsb1101-932  1
2001 Deutschman WA, Dahlquist FW. Thermodynamic basis for the increased thermostability of CheY from the hyperthermophile Thermotoga maritima. Biochemistry. 40: 13107-13. PMID 11669649 DOI: 10.1021/bi010665t  1
2001 Ryan M, Liu T, Dahlquist FW, Griffith OH. A catalytic diad involved in substrate-assisted catalysis: NMR study of hydrogen bonding and dynamics at the active site of phosphatidylinositol-specific phospholipase C. Biochemistry. 40: 9743-50. PMID 11583175 DOI: 10.1021/bi010958m  1
2001 Skrynnikov NR, Mulder FA, Hon B, Dahlquist FW, Kay LE. Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: application to methionine residues in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society. 123: 4556-66. PMID 11457242 DOI: 10.1021/ja004179p  1
2001 Mulder FA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE. Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society. 123: 967-75. PMID 11456632 DOI: 10.1021/ja003447g  1
2001 Goto NK, Skrynnikov NR, Dahlquist FW, Kay LE. What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR. Journal of Molecular Biology. 308: 745-64. PMID 11350172 DOI: 10.1006/jmbi.2001.4614  1
2001 Giesen AW, Bae LC, Barrett CL, Chyba JA, Chaykovsky MM, Cheng MC, Murray JH, Oliver EJ, Sullivan SM, Brown JM, Dahlquist FW, Homans SW. Measurement of one-bond 1H-13C, couplings in backbone-labelled proteins. Journal of Biomolecular Nmr. 19: 255-60. PMID 11330812 DOI: 10.1023/A:1011298531256  1
2000 Mulder FA, Hon B, Muhandiram DR, Dahlquist FW, Kay LE. Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR. Biochemistry. 39: 12614-22. PMID 11027141 DOI: 10.1021/bi001351t  1
2000 Anderson JS, Forman MD, Modleski S, Dahlquist FW, Baxter SM. Cooperative ordering in homeodomain-DNA recognition: solution structure and dynamics of the MATa1 homeodomain. Biochemistry. 39: 10045-54. PMID 10955992 DOI: 10.1021/bi000677z  1
2000 Halkides CJ, McEvoy MM, Casper E, Matsumura P, Volz K, Dahlquist FW. The 1.9 A resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY. Biochemistry. 39: 5280-6. PMID 10819997 DOI: 10.1021/bi9925524  1
2000 Barrick D, Dahlquist FW. Trans-substitution of the proximal hydrogen bond in myoglobin: I. Structural consequences of hydrogen bond deletion. Proteins. 39: 278-90. PMID 10813811 DOI: 10.1002/(SICI)1097-0134(20000601)39:4<278::AID-PROT20>3.0.CO;2-T  1
2000 Yang G, Cecconi C, Baase WA, Vetter IR, Breyer WA, Haack JA, Matthews BW, Dahlquist FW, Bustamante C. Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme. Proceedings of the National Academy of Sciences of the United States of America. 97: 139-44. PMID 10618384 DOI: 10.1073/pnas.97.1.139  1
1999 Gassner NC, Baase WA, Lindstrom JD, Lu J, Dahlquist FW, Matthews BW. Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry. 38: 14451-60. PMID 10545167 DOI: 10.1021/bi9915519  1
1999 Llinás M, Gillespie B, Dahlquist FW, Marqusee S. The energetics of T4 lysozyme reveal a hierarchy of conformations. Nature Structural Biology. 6: 1072-8. PMID 10542101 DOI: 10.1038/14956  1
1999 McEvoy MM, Bren A, Eisenbach M, Dahlquist FW. Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein fliM. Journal of Molecular Biology. 289: 1423-33. PMID 10373376 DOI: 10.1006/jmbi.1999.2830  1
1999 Bertelsen EB, Zhou H, Lowry DF, Flynn GC, Dahlquist FW. Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution. Protein Science : a Publication of the Protein Society. 8: 343-54. PMID 10048327 DOI: 10.1110/ps.8.2.343  1
1999 Liu T, Ryan M, Dahlquist FW, Griffith OH. Characterization of the histidine residues of B. cereus phosphatidylinositol-specific phospholipase C by NMR Acs Symposium Series. 718: 91-108.  1
1998 Blat Y, Gillespie B, Bren A, Dahlquist FW, Eisenbach M. Regulation of phosphatase activity in bacterial chemotaxis. Journal of Molecular Biology. 284: 1191-9. PMID 9837737 DOI: 10.1006/jmbi.1998.2224  1
1998 Halkides CJ, Zhu X, Phillion DP, Matsumura P, Dahlquist FW. Synthesis and biochemical characterization of an analogue of CheY-phosphate, a signal transduction protein in bacterial chemotaxis. Biochemistry. 37: 13674-80. PMID 9753454 DOI: 10.1021/bi9806293  1
1998 McEvoy MM, Hausrath AC, Randolph GB, Remington SJ, Dahlquist FW. Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway. Proceedings of the National Academy of Sciences of the United States of America. 95: 7333-8. PMID 9636149 DOI: 10.1073/pnas.95.13.7333  1
1998 Usher KC, de la Cruz AF, Dahlquist FW, Swanson RV, Simon MI, Remington SJ. Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability. Protein Science : a Publication of the Protein Society. 7: 403-12. PMID 9521117 DOI: 10.1002/pro.5560070221  1
1998 Daughdrill GW, Hanely LJ, Dahlquist FW. The C-terminal half of the anti-sigma factor FlgM contains a dynamic equilibrium solution structure favoring helical conformations. Biochemistry. 37: 1076-82. PMID 9454599 DOI: 10.1021/bi971952t  1
1998 Bertelsen EB, Zhou H, Flynn GC, Dahlquist FW. NMR characterization of the c-terminal 10 kda domain of dnak Faseb Journal. 12: A1417.  1
1997 McEvoy MM, Dahlquist FW. Phosphohistidines in bacterial signaling. Current Opinion in Structural Biology. 7: 793-7. PMID 9434897 DOI: 10.1016/S0959-440X(97)80148-0  1
1997 Liu T, Ryan M, Dahlquist FW, Griffith OH. Determination of pKa values of the histidine side chains of phosphatidylinositol-specific phospholipase C from Bacillus cereus by NMR spectroscopy and site-directed mutagenesis. Protein Science : a Publication of the Protein Society. 6: 1937-44. PMID 9300493 DOI: 10.1002/pro.5560060914  1
1997 Feher VA, Zapf JW, Hoch JA, Whiteley JM, McIntosh LP, Rance M, Skelton NJ, Dahlquist FW, Cavanagh J. High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: implications for phosphorylation and molecular recognition. Biochemistry. 36: 10015-25. PMID 9254596 DOI: 10.1021/bi970816l  1
1997 Wilkens S, Dunn SD, Chandler J, Dahlquist FW, Capaldi RA. Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase. Nature Structural Biology. 4: 198-201. PMID 9164460 DOI: 10.1038/nsb0397-198  1
1997 Hall DA, Maus DC, Gerfen GJ, Inati SJ, Becerra LR, Dahlquist FW, Griffin RG. Polarization-enhanced NMR spectroscopy of biomolecules in frozen solution. Science (New York, N.Y.). 276: 930-2. PMID 9139651 DOI: 10.1126/science.276.5314.930  1
1997 Daughdrill GW, Chadsey MS, Karlinsey JE, Hughes KT, Dahlquist FW. The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28. Nature Structural Biology. 4: 285-91. PMID 9095196 DOI: 10.1038/nsb0497-285  1
1997 Zhou H, Dahlquist FW. Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR. Biochemistry. 36: 699-710. PMID 9020767 DOI: 10.1021/bi961663p  1
1997 Barrick D, Ho NT, Simplaceanu V, Dahlquist FW, Ho C. A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin. Nature Structural Biology. 4: 78-83. PMID 8989328 DOI: 10.1038/nsb0197-78  1
1997 McEvoy MM, de la Cruz AF, Dahlquist FW. Large modular proteins by NMR. Nature Structural Biology. 4: 9. PMID 8989314 DOI: 10.1038/nsb0197-9  1
1996 Feher VA, Baldwin EP, Dahlquist FW. Access of ligands to cavities within the core of a protein is rapid. Nature Structural Biology. 3: 516-21. PMID 8646537 DOI: 10.1038/nsb0696-516  1
1996 McEvoy MM, Muhandiram DR, Kay LE, Dahlquist FW. Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy. Biochemistry. 35: 5633-40. PMID 8639521 DOI: 10.1021/bi952707h  1
1996 Zhou H, McEvoy MM, Lowry DF, Swanson RV, Simon MI, Dahlquist FW. Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker. Biochemistry. 35: 433-43. PMID 8555213 DOI: 10.1021/bi951960e  1
1995 Feher VA, Zapf JW, Hoch JA, Dahlquist FW, Whiteley JM, Cavanagh J. 1H, 15N, and 13C backbone chemical shift assignments, secondary structure, and magnesium-binding characteristics of the Bacillus subtilis response regulator, Spo0F, determined by heteronuclear high-resolution NMR. Protein Science : a Publication of the Protein Society. 4: 1801-14. PMID 8528078 DOI: 10.1002/pro.5560040915  1
1995 Matthews BW, Morton AG, Dahlquist FW. Use of NMR to detect water within nonpolar protein cavities. Science (New York, N.Y.). 270: 1847-9. PMID 8525384 DOI: 10.1126/science.270.5243.1847  1
1995 Fischer MW, Majumdar A, Dahlquist FW, Zuiderweg ER. 15N, 13C, and 1H NMR assignments and secondary structure for T4-lysozyme. Journal of Magnetic Resonance. Series B. 108: 143-54. PMID 7648012 DOI: 10.1006/jmrb.1995.1115  1
1995 Wilkens S, Dahlquist FW, McIntosh LP, Donaldson LW, Capaldi RA. Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy. Nature Structural Biology. 2: 961-7. PMID 7583669 DOI: 10.1038/nsb1195-961  1
1995 McEvoy MM, Zhou H, Roth AF, Lowry DF, Morrison TB, Kay LE, Dahlquist FW. Nuclear magnetic resonance assignments and global fold of a CheY-binding domain in CheA, the chemotaxis-specific kinase of Escherichia coli. Biochemistry. 34: 13871-80. PMID 7577981  1
1995 Zhou H, Lowry DF, Swanson RV, Simon MI, Dahlquist FW. NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherichia coli: assignments, secondary structure, general fold, and backbone dynamics. Biochemistry. 34: 13858-70. PMID 7577980  1
1995 Swanson RV, Lowry DF, Matsumura P, McEvoy MM, Simon MI, Dahlquist FW. Localized perturbations in CheY structure monitored by NMR identify a CheA binding interface. Nature Structural Biology. 2: 906-10. PMID 7552716  1
1994 Cavanagh J, Zapf J, Hoch JA, Feher V, Dahlquist FW, Whiteley JM. Aspartyl phosphates in the regulatory control of bacterial response. Amino Acids. 6: 131-40. PMID 24190783 DOI: 10.1007/BF00805841  1
1994 Heinz DW, Baase WA, Zhang XJ, Blaber M, Dahlquist FW, Matthews BW. Accommodation of amino acid insertions in an alpha-helix of T4 lysozyme. Structural and thermodynamic analysis. Journal of Molecular Biology. 236: 869-86. PMID 8114100 DOI: 10.1006/jmbi.1994.1195  1
1994 Moy FJ, Lowry DF, Matsumura P, Dahlquist FW, Krywko JE, Domaille PJ. Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy. Biochemistry. 33: 10731-42. PMID 8075074  0.4
1994 Phillips CL, Stark MR, Johnson AD, Dahlquist FW. Heterodimerization of the yeast homeodomain transcriptional regulators alpha 2 and a1 induces an interfacial helix in alpha 2. Biochemistry. 33: 9294-302. PMID 8049230  1
1994 Lowry DF, Roth AF, Rupert PB, Dahlquist FW, Moy FJ, Domaille PJ, Matsumura P. Signal transduction in chemotaxis. A propagating conformation change upon phosphorylation of CheY. The Journal of Biological Chemistry. 269: 26358-62. PMID 7929354  1
1994 Baxter SM, Gontrum DM, Phillips CL, Roth AF, Dahlquist FW. Heterodimerization of the yeast homeodomain transcriptional regulators alpha 2 and a1: secondary structure determination of the a1 homeodomain and changes produced by alpha 2 interactions. Biochemistry. 33: 15309-20. PMID 7803394  1
1994 Yamazaki T, Lee W, Revington M, Mattiello DL, Dahlquist FW, Arrowsmith CH, Kay LE. An HNCA pulse scheme for the backbone assignment of 15N,13C,2H-labeled proteins: Application to a 37-kDa Trp repressor-DNA complex Journal of the American Chemical Society. 116: 6464-6465.  1
1993 Heinz DW, Baase WA, Dahlquist FW, Matthews BW. How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme. Nature. 361: 561-4. PMID 8429913 DOI: 10.1038/361561a0  1
1993 Flynn GC, Beckers CJ, Baase WA, Dahlquist FW. Individual subunits of bacterial luciferase are molten globules and interact with molecular chaperones. Proceedings of the National Academy of Sciences of the United States of America. 90: 10826-30. PMID 7902573  1
1992 Lu J, Dahlquist FW. Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR. Biochemistry. 31: 4749-56. PMID 1591236  1
1992 Lu J, Baase WA, Muchmore DC, Dahlquist FW. Protein folding: assignment of the energetic changes of reversible chemical modifications to the folded or unfolded states. Biochemistry. 31: 7765-72. PMID 1510962  1
1992 Gegner JA, Graham DR, Roth AF, Dahlquist FW. Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway. Cell. 70: 975-82. PMID 1326408 DOI: 10.1016/0092-8674(92)90247-A  1
1991 Rice MS, Dahlquist FW. Sites of deamidation and methylation in Tsr, a bacterial chemotaxis sensory transducer. The Journal of Biological Chemistry. 266: 9746-53. PMID 2033064  1
1991 Gegner JA, Dahlquist FW. Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA. Proceedings of the National Academy of Sciences of the United States of America. 88: 750-4. PMID 1992467  1
1991 Dao-pin S, Anderson DE, Baase WA, Dahlquist FW, Matthews BW. Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. Biochemistry. 30: 11521-9. PMID 1747370  0.32
1991 Prosser RS, Davis JH, Dahlquist FW, Lindorfer MA. 2H nuclear magnetic resonance of the gramicidin A backbone in a phospholipid bilayer. Biochemistry. 30: 4687-96. PMID 1709361  1
1991 Phillips CL, Vershon AK, Johnson AD, Dahlquist FW. Secondary structure of the homeo domain of yeast alpha 2 repressor determined by NMR spectroscopy. Genes & Development. 5: 764-72. PMID 1673952  1
1991 Schmieder P, Thanabal V, McIntosh LP, Dahlquist FW, Wagner G. Measurements of Hα-HN vicinal coupling constants in a protein with large line widths in a new 3D 1H-15N-13C quadruple resonance NMR experiment Journal of the American Chemical Society. 113: 6323-6324.  1
1990 Anderson DE, Becktel WJ, Dahlquist FW. pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry. 29: 2403-8. PMID 2337607  1
1990 Oas TG, McIntosh LP, O'Shea EK, Dahlquist FW, Kim PS. Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy. Biochemistry. 29: 2891-4. PMID 2337572  1
1990 McIntosh LP, Wand AJ, Lowry DF, Redfield AG, Dahlquist FW. Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme. Biochemistry. 29: 6341-62. PMID 2207079  1
1990 Stewart RC, Roth AF, Dahlquist FW. Mutations that affect control of the methylesterase activity of CheB, a component of the chemotaxis adaptation system in Escherichia coli. Journal of Bacteriology. 172: 3388-99. PMID 2188960  1
1990 McIntosh LP, Dahlquist FW. Biosynthetic incorporation of 15N and 13C for assignment and interpretation of nuclear magnetic resonance spectra of proteins. Quarterly Reviews of Biophysics. 23: 1-38. PMID 2188278 DOI: 10.1017/S0033583500005400  1
1990 Zuiderweg ERP, McIntosh LP, Dahlquist FW, Fesik SW. Three-dimensional 13C-resolved proton NOE spectroscopy of uniformly 13C-labeled proteins for the NMR assignment and structure determination of larger molecules Journal of Magnetic Resonance (1969). 86: 210-216. DOI: 10.1016/0022-2364(90)90228-2  1
1990 Fesik SW, Eaton HL, Olejniczak ET, Zuiderweg ERP, McIntosh LP, Dahlquist FW. 2D and 3D NMR spectroscopy employing 13C-13C magnetization transfer by isotropic mixing. Spin system identification in large proteins Journal of the American Chemical Society. 112: 886-888.  1
1989 Muchmore DC, McIntosh LP, Russell CB, Anderson DE, Dahlquist FW. Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance. Methods in Enzymology. 177: 44-73. PMID 2691846 DOI: 10.1016/0076-6879(89)77005-1  1
1989 Weaver LH, Gray TM, Grütter MG, Anderson DE, Wozniak JA, Dahlquist FW, Matthews BW. High-resolution structure of the temperature-sensitive mutant of phage lysozyme, Arg 96----His. Biochemistry. 28: 3793-7. PMID 2665808  1
1989 Russell CB, Stewart RC, Dahlquist FW. Control of transducer methylation levels in Escherichia coli: investigation of components essential for modulation of methylation and demethylation reactions. Journal of Bacteriology. 171: 3609-18. PMID 2661528  1
1989 Russell CB, Dahlquist FW. Exchange of chromosomal and plasmid alleles in Escherichia coli by selection for loss of a dominant antibiotic sensitivity marker. Journal of Bacteriology. 171: 2614-8. PMID 2651409  1
1989 Russell CB, Thaler DS, Dahlquist FW. Chromosomal transformation of Escherichia coli recD strains with linearized plasmids. Journal of Bacteriology. 171: 2609-13. PMID 2651408  1
1989 Redfield AG, McIntosh LP, Dahlquist FW. Use of 13C and 15N isotope labels for proton nuclear magnetic resonance and nuclear Overhauser effect. Structural and dynamic studies of larger proteins and nucleic acids. Archivos De Biología Y Medicina Experimentales. 22: 129-37. PMID 2619316  1
1989 Oas TG, Hartzell CJ, Drobny GP, Dahlquist FW. Selective NMR detection of 13C15N dipole pairs in solid samples Journal of Magnetic Resonance (1969). 81: 395-399. DOI: 10.1016/0022-2364(89)90072-3  1
1988 Stewart RC, Russell CB, Roth AF, Dahlquist FW. Interaction of CheB with chemotaxis signal transduction components in Escherichia coli: modulation of the methylesterase activity and effects on cell swimming behavior. Cold Spring Harbor Symposia On Quantitative Biology. 53: 27-40. PMID 3076082  1
1988 Stewart RC, Dahlquist FW. N-terminal half of CheB is involved in methylesterase response to negative chemotactic stimuli in Escherichia coli. Journal of Bacteriology. 170: 5728-38. PMID 3056911  1
1988 Lowry DF, Redfield AG, McIntosh LP, Dahlquist FW. One-dimensional Nuclear Overhauser Effect with two-dimensional heteronuclear multiple quantum coherence detection: Proton-proton nitrogen-15 correlation in T4 lysozyme Journal of the American Chemical Society. 110: 6885-6886.  1
1987 McIntosh LP, Dahlquist FW, Redfield AG. Proton NMR and NOE structural and dynamic studies of larger proteins and nucleic acids aided by isotope labels: T4 lysozyme. Journal of Biomolecular Structure & Dynamics. 5: 21-34. PMID 3271466 DOI: 10.1080/07391102.1987.10506372  1
1987 McIntosh LP, Griffey RH, Muchmore DC, Nielson CP, Redfield AG, Dahlquist FW. Proton NMR measurements of bacteriophage T4 lysozyme aided by 15N isotopic labeling: structural and dynamic studies of larger proteins. Proceedings of the National Academy of Sciences of the United States of America. 84: 1244-8. PMID 3029773 DOI: 10.1073/pnas.84.5.1244  1
1987 Oas TG, Hartzell CJ, Dahlquist FW, Drobny GP. The amide 15N chemical shift tensors of four peptides determined from 13C dipole-coupled chemical shift powder patterns Journal of the American Chemical Society. 109: 5962-5966.  1
1987 Stewart RC, Dahlquist FW. Molecular components of bacterial chemotaxis Chemical Reviews. 87: 997-1025.  1
1987 Oas TG, Hartzell CJ, McMahon TJ, Drobny GP, Dahlquist FW. The carbonyl 13C chemical shift tensors of five peptides determined from 15N dipole-coupled chemical shift powder patterns Journal of the American Chemical Society. 109: 5956-5962.  1
1986 Griffey RH, Redfield AG, McIntosh LP, Oas TG, Dahlquist FW. Assignment of proton amide resonances of T4 lysozyme by 13C and 15N multiple isotopic labeling Journal of the American Chemical Society. 108: 6816-6817.  1
1985 Paddy MR, Dahlquist FW, Dratz EA, Deese AJ. Simultaneous observation of order and dynamics at several defined positions in a single acyl chain using 2H NMR of single acyl chain perdeuterated phosphatidylcholines. Biochemistry. 24: 5988-95. PMID 4084502  1
1985 Kehry MR, Doak TG, Dahlquist FW. Aberrant regulation of methylesterase activity in cheD chemotaxis mutants of Escherichia coli. Journal of Bacteriology. 161: 105-12. PMID 3917995  1
1985 Kehry MR, Doak TG, Dahlquist FW. Sensory adaptation in bacterial chemotaxis: regulation of demethylation. Journal of Bacteriology. 163: 983-90. PMID 3897203  1
1985 Wilson ML, Dahlquist FW. Membrane protein conformational change dependent on the hydrophobic environment. Biochemistry. 24: 1920-8. PMID 3893541  1
1985 Griffey RH, Redfield AG, Loomis RE, Dahlquist FW. Nuclear magnetic resonance observation and dynamics of specific amide protons in T4 lysozyme. Biochemistry. 24: 817-22. PMID 3888265  1
1985 Russell CB, Dahlquist FW. Evidence for a regulator of methyl esterase in bacterial chemotaxis Federation Proceedings. 44: No. 7927.  1
1984 Kehry MR, Doak TG, Dahlquist FW. Stimulus-induced changes in methylesterase activity during chemotaxis in Escherichia coli. The Journal of Biological Chemistry. 259: 11828-35. PMID 6384215  1
1983 Christen R, Schackmann RW, Dahlquist FW, Shapiro BM. 31P-NMR analysis of sea urchin sperm activation. Reversible formation of high energy phosphate compounds by changes in intracellular pH. Experimental Cell Research. 149: 289-94. PMID 6641799 DOI: 10.1016/0014-4827(83)90400-7  1
1983 Kehry MR, Wilson ML, Dahlquist FW. A simple quantitative method for the determination of 3-fluorotyrosine substitution in proteins. Analytical Biochemistry. 131: 236-41. PMID 6614455 DOI: 10.1016/0003-2697(83)90160-4  1
1983 Kehry MR, Bond MW, Hunkapiller MW, Dahlquist FW. Enzymatic deamidation of methyl-accepting chemotaxis proteins in Escherichia coli catalyzed by the cheB gene product. Proceedings of the National Academy of Sciences of the United States of America. 80: 3599-603. PMID 6304723  1
1983 Kehry MR, Engstrom P, Dahlquist FW, Hazelbauer GL. Multiple covalent modifications of Trg, a sensory transducer of Escherichia coli Journal of Biological Chemistry. 258: 5050-5055. PMID 6300110  1
1982 Anderson DC, Dahlquist FW. Biphasic transient kinetics are a property of a single site in horse liver alcohol dehydrogenase Biochemistry. 21: 3578-3584. PMID 7052126  1
1982 Anderson DC, Dahlquist FW. Properties of bound trifluoroethanol complexes with horse liver alcohol dehydrogenase Biochemistry. 21: 3569-3578. PMID 7052125  1
1982 Huskins KR, Bernhard SA, Dahlquist FW. Halibut muscle 3-phosphoglycerate kinase. Chemical and physical properties of the enzyme and its substrate complexes Biochemistry. 21: 4180-4188. PMID 6982068  1
1982 Kehry MR, Dahlquist FW. Adaptation in bacterial chemotaxis: CheB-dependent modification permits additional methylations of sensory transducer proteins Cell. 29: 761-772. PMID 6758950 DOI: 10.1016/0092-8674(82)90438-X  1
1982 Anderson DC, Wilson ML, Dahlquist FW. Fluorinated ligands as nuclear magnetic resonance probes of active-site nonequivalence in abortive ternary complexes of horse liver alcohol dehydrogenase Biochemistry. 21: 4664-4670. PMID 6753924  1
1982 Anderson DC, Dahlquist FW. 19F nuclear magnetic resonance observations of aldehyde dismutation catalyzed by horse liver alcohol dehydrogenase Archives of Biochemistry and Biophysics. 217: 226-235. PMID 6751236 DOI: 10.1016/0003-9861(82)90497-0  1
1982 Kehry MR, Dahlquist FW. The methyl-accepting chemotaxis proteins of Escherichia coli. Identification of the multiple methylation sites on methyl-accepting chemotaxis protein I Journal of Biological Chemistry. 257: 10378-10386. PMID 6213619  1
1981 Deese AJ, Dratz EA, Dahlquist FW, Paddy MR. Interaction of rhodopsin with two unsaturated phosphatidylcholines: A deuterium nuclear magnetic resonance study Biochemistry. 20: 6420-6427. PMID 7306517  1
1981 Chelsky D, Dahlquist FW. Multiple sites of methylation in the methyl accepting chemotaxis proteins of Escherichia coli Progress in Clinical and Biological Research. 63: 371-381. PMID 7031684  1
1981 Rollins C, Dahlquist FW. The methyl-accepting chemotaxis proteins of E. coli: A repellent-stimulated, covalent modification, distinct from methylation Cell. 25: 333-340. PMID 7026041 DOI: 10.1016/0092-8674(81)90051-9  1
1981 Chelsky D, Dahlquist FW. Methyl-accepting chemotaxis proteins of Escherichia coli: Methylated at three sites in a single tryptic fragment Biochemistry. 20: 977-982. PMID 7011380  1
1981 Kallas T, Dahlquist FW. Phosphorus-31 nuclear magnetic resonance analysis of internal pH during photosynthesis in the cyanobacterium Synechococcus Biochemistry. 20: 5900-5907. PMID 6794618  1
1981 Paddy MR, Dahlquist FW, Davis JH, Bloom M. Dynamical and temperature-dependent effects of lipid-protein interactions. Application of deuterium nuclear magnetic resonance and electron paramagnetic resonance spectroscopy to the same reconstitutions of cytochrome c oxidase. Biochemistry. 20: 3152-62. PMID 6264951  1
1981 Liu RSH, Matsumoto H, Asato AE, Denny M, Shichida Y, Yoshizawa T, Dahlquist FW. Synthesis and properties of 12-fluororetinal and 12-fluororhodopsin. A model system for 19F NMR studies of visual pigments Journal of the American Chemical Society. 103: 7195-7201.  1
1980 Anderson DC, Dahlquist FW. Determination of the equilibrium distribution between alcohol and aldehyde substrates when bound to horse liver alcohol dehydrogenase using magnetic resonance Biochemistry. 19: 5486-5493. PMID 7006685  1
1980 Chelsky D, Dahlquist FW. Structural studies of methyl-accepting chemotaxis proteins of Escherichia coli: Evidence for multiple methylation sites Proceedings of the National Academy of Sciences of the United States of America. 77: 2434-2438. PMID 6994098  1
1980 Rollins CM, Dahlquist FW. Methylation of chemotaxis-specific proteins in Escherichia coli cells permeable to S-adenosylmethionine Biochemistry. 19: 4627-4632. PMID 6775692  1
1980 Chelsky D, Dahlquist FW. Chemotaxis in Escherichia coli: Associations of protein components Biochemistry. 19: 4633-4639. PMID 6448631  1
1980 Swanson PE, Paddy MR, Dahlquist FW, Storm DR. Characterization of octapeptin-membrane interactions using spin-labeled octapeptin Biochemistry. 19: 3307-3314. PMID 6250564  1
1979 Anderson DC, Dahlquist FW. A convenient large scale preparation of the EE isozyme of horse liver alcohol dehydrogenase Analytical Biochemistry. 99: 392-398. PMID 517749 DOI: 10.1016/S0003-2697(79)80023-8  1
1979 Muchmore DC, Dahlquist FW. The monothioacetal group, a new cleavable center for cross-linking reagents Biochemical and Biophysical Research Communications. 86: 599-604. PMID 426806 DOI: 10.1016/0006-291X(79)91755-8  1
1978 Dahlquist FW. The meaning of Scatchard and Hill plots Methods in Enzymology. 48: 270-299. PMID 345049  1
1977 Dahlquist FW, Muchmore DC, Davis JH, Bloom M. Deuterium magnetic resonance studies of the interaction of lipids with membrane proteins. Proceedings of the National Academy of Sciences of the United States of America. 74: 5435-9. PMID 202955  1
1977 Longmuir KJ, Capaldi RA, Dahlquist FW. Nuclear magnetic resonance studies of lipid-protein interactions. A model of the dynamics and energetics of phosphatidylcholine bilayers that contain cytochrome c oxidase Biochemistry. 16: 5746-5755. PMID 201275  1
1977 Long JW, Dahlquist FW. Evidence for induced interactions in the anticooperative binding of nicotinamide adenine dinucleotide to sturgeon muscle glyceraldehyde-3-phosphate dehydrogenase Biochemistry. 16: 3792-3797. PMID 197986  1
1977 Bigbee WL, Dahlquist FW. Magnetic resonance investigation of ionizable residues at the active site of thermolysin Biochemistry. 16: 3798-3803. PMID 20127  1
1976 Longmuir KJ, Dahlquist FW. Direct spectroscopic observation of inner and outer hydrocarbon chains of lipid bilayer vesicles Proceedings of the National Academy of Sciences of the United States of America. 73: 2716-2719. PMID 1066684  1
1976 Dahlquist FW, Long JW, Bigbee WL. Role of calcium in the thermal stability of thermolysin Biochemistry. 15: 1103-1111. PMID 814920  1
1976 Dahlquist FW, Elwell RA, Lovely PS. Studies of bacterial chemotaxis in defined concentration gradients. A model for chemotaxis toward L serine Journal of Supramolecular and Cellular Biochemistry. 4: 329-342. PMID 772315  1
1975 Lovely PS, Dahlquist FW. Statistical measures of bacterial motility and chemotaxis Journal of Theoretical Biology. 50: 477-496. PMID 1094203 DOI: 10.1016/0022-5193(75)90094-6  1
1975 Dahlquist FW, Purich DL. Regulation of Escherichia coli glutamine synthetase. Evidence for the action of some feedback modifiers at the active site of the unadenylylated enzyme Biochemistry. 14: 1980-1989. PMID 235974  1
1975 Mueggler PA, Dahlquist FW, Wolfe RG. Malate dehydrogenase, anticooperative NADH, and L-malate binding in ternary complexes with supernatant pig heart enzyme Biochemistry. 14: 3490-3497. PMID 167827  1
1975 Dahlquist FW, Longmuir K, Vernet RBD. Direct observation of chemical exchange by a selective pulse NMR technique Journal of Magnetic Resonance (1969). 17: 406-410. DOI: 10.1016/0022-2364(75)90210-3  1
1974 Lovely P, Dahlquist FW, Macnab R, Koshland DE. An instrument for recording the motions of microorganisms in chemical gradients Review of Scientific Instruments. 45: 683-686. PMID 4596820 DOI: 10.1063/1.1686713  1
1974 Dahlquist FW. The quantitative interpretation of maximum in Scatchard plots Febs Letters. 49: 267-268. PMID 4442606 DOI: 10.1016/0014-5793(74)80527-2  1
1974 Bigbee WL, Dahlquist FW. Magnetic resonance studies of the active-site region of thermolysin Biochemistry. 13: 3542-3549. PMID 4367427  1
1973 Matthews BW, Dahlquist FW, Maynard AY. Crystallographic data for lysozyme from bacteriophage T4 Journal of Molecular Biology. 78: 575-576. PMID 4754847 DOI: 10.1016/0022-2836(73)90478-6  1
1972 Dahlquist FW, Lovely P, Koshland DE. Quantitative analysis of bacterial migration in chemotaxis Nature: New Biology. 236: 120-123. PMID 4554379  1
1969 Raftery MA, Rand-Meir T, Dahlquist FW, Parsons SM, Borders CL, Wolcott RG, Beranek W, Jao L. Separation of glycosaminoglycan saccharide and glycoside mixtures by gel filtration. Analytical Biochemistry. 30: 427-35. PMID 5821304  1
1969 Dahlquist FW, Borders CL, Jacobson G, Raftery MA. The stereospecificity of human, hen, and papaya lysozymes. Biochemistry. 8: 694-700. PMID 5815782  1
1969 Dahlquist FW, Raftery MA. Some properties of contiguous binding subsites on lysozyme as determined by proton magnetic resonance spectroscopy. Biochemistry. 8: 713-25. PMID 5793721  1
1969 Parsons SM, Jao L, Dahlquist FW, Borders CL, Racs J, Groff T, Raftery MA. The nature of amino acid side chains which are critical for the activity of lysozyme. Biochemistry. 8: 700-12. PMID 5793720  1
1969 Dahlquist FW, Rand-Meir T, Raftery MA. Application of secondary alpha-deuterium kinetic isotope effects to studies of enzyme catalysis. Glycoside hydrolysis by lysozyme and beta-glucosidase. Biochemistry. 8: 4214-21. PMID 5388150  1
1969 Rand-Meir T, Dahlquist FW, Raftery MA. Use of synthetic substrates to study binding and catalysis by lysozyme. Biochemistry. 8: 4206-14. PMID 5346398  1
1969 Raftery MA, Dahlquist FW, Parsons SM, Wolcott RG. The use of nuclear magnetic resonance to describe relative modes of binding to lysozyme of homologous inhibitors and related substrates. Proceedings of the National Academy of Sciences of the United States of America. 62: 44-51. PMID 5253664  1
1969 Raftery MA, Dahlquist FW. The chemistry of lysozyme. Fortschritte Der Chemie Organischer Naturstoffe = Progress in the Chemistry of Organic Natural Products. ProgrèS Dans La Chimie Des Substances Organiques Naturelles. 27: 340-81. PMID 4908211  1
1968 Dahlquist FW, Raftery MA. A nuclear magnetic resonance study of enzyme-inhibitor association. The use of pH and temperature effects to probe the binding environments. Biochemistry. 7: 3277-80. PMID 5684349  1
1968 Dahlquist FW, Raftery MA. A nuclear magnetic resonance study of association equilibria and enzyme-boud environments of N-acetyl-D-glucosamine anomers and lysozyme. Biochemistry. 7: 3269-76. PMID 5684348  1
1968 Raftery MA, Dahlquist FW, Chan SI, Parsons SM. A proton magnetic resonance study of the association of lysozyme with monosaccharide inhibitors. The Journal of Biological Chemistry. 243: 4175-80. PMID 5679957  1
1968 Dahlquist FW, Rand-Meir T, Raftery MA. Demonstration of carbonium ion intermediate during lysozyme catalysis. Proceedings of the National Academy of Sciences of the United States of America. 61: 1194-8. PMID 5249805  1
1967 Dahlquist FW, Raftery M. Specificity of cleavage of chitotriose by lysozyme [41] Nature. 213: 625-626. DOI: 10.1038/213625a0  1
1966 Dahlquist FW, Jao L, Raftery M. On the binding of chitin oligosaccharides to lysozyme. Proceedings of the National Academy of Sciences of the United States of America. 56: 26-30. PMID 5229853  1
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