R. Brian Dyer - Publications

Affiliations: 
Chemistry Emory University, Atlanta, GA 
Website:
https://scholarblogs.emory.edu/dyerlab/group/brian-dyer/

68 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 Sanchez MLK, Wu CH, Adams MWW, Dyer RB. Optimizing electron transfer from CdSe QDs to hydrogenase for photocatalytic H production. Chemical Communications (Cambridge, England). PMID 30997456 DOI: 10.1039/c9cc01150a  1
2018 Zhao J, Su H, Vansuch GE, Liu Z, Salaita K, Dyer RB. Localized Nanoscale Heating Leads to Ultrafast Hydrogel Volume-Phase Transition. Acs Nano. PMID 30574782 DOI: 10.1021/acsnano.8b07150  1
2018 Su H, Liu Z, Liu Y, Ma VP, Blanchard A, Zhao J, Galior K, Dyer RB, Salaita K. Light-Responsive Polymer Particles as Force Clamps for the Mechanical Unfolding of Target Molecules. Nano Letters. PMID 29589759 DOI: 10.1021/acs.nanolett.8b00459  1
2017 Reid KA, Davis CM, Brian Dyer R, Kindt JT. Binding, folding and insertion of a β-hairpin peptide at a lipid bilayer surface: Influence of electrostatics and lipid tail packing. Biochimica Et Biophysica Acta. PMID 29291379 DOI: 10.1016/j.bbamem.2017.12.019  0.36
2017 Greene BL, Vansuch GE, Chica BC, Adams MWW, Dyer RB. Applications of Photogating and Time Resolved Spectroscopy to Mechanistic Studies of Hydrogenases. Accounts of Chemical Research. PMID 29083854 DOI: 10.1021/acs.accounts.7b00356  1
2016 Greene BL, Vansuch GE, Wu CH, Adams MW, Dyer RB. Glutamate Gated Proton-Coupled Electron Transfer Activity of a [NiFe]-Hydrogenase. Journal of the American Chemical Society. PMID 27617712 DOI: 10.1021/jacs.6b07789  1
2016 Greene BL, Wu CH, Vansuch GE, Adams MW, Dyer RB. Proton Inventory and Dynamics in the Nia-S to Nia-C Transition of a [NiFe]-Hydrogenase. Biochemistry. PMID 26956769 DOI: 10.1021/acs.biochem.5b01348  1
2016 Reddish MJ, Vaughn MB, Fu R, Dyer RB. Ligand-Dependent Conformational Dynamics of Dihydrofolate Reductase. Biochemistry. 55: 1485-93. PMID 26901612 DOI: 10.1021/acs.biochem.5b01364  1
2016 Karahalis GJ, Thangavel A, Chica B, Bacsa J, Dyer RB, Scarborough CC. Synthesis and Catalytic Reactivity of a Dicopper(II) μ-η(2):η(2)-Peroxo Species Supported by 1,4,7-Tri-tert-butyl-1,4,7-triazacyclononane. Inorganic Chemistry. PMID 26789550 DOI: 10.1021/acs.inorgchem.5b02205  1
2016 Davis CM, Dyer RB. The Role of Electrostatic Interactions in Folding of β-Proteins. Journal of the American Chemical Society. PMID 26750867 DOI: 10.1021/jacs.5b13201  1
2015 Greene BL, Wu CH, McTernan PM, Adams MW, Dyer RB. Proton-coupled electron transfer dynamics in the catalytic mechanism of a [NiFe]-hydrogenase. Journal of the American Chemical Society. 137: 4558-66. PMID 25790178 DOI: 10.1021/jacs.5b01791  1
2015 Davis CM, Cooper AK, Dyer RB. Fast helix formation in the B domain of protein A revealed by site-specific infrared probes. Biochemistry. 54: 1758-66. PMID 25706439 DOI: 10.1021/acs.biochem.5b00037  1
2015 Callender R, Dyer RB. The dynamical nature of enzymatic catalysis. Accounts of Chemical Research. 48: 407-13. PMID 25539144 DOI: 10.1021/ar5002928  1
2015 Einarsdóttir O, McDonald W, Funatogawa C, Szundi I, Woodruff WH, Dyer RB. The pathway of O₂to the active site in heme-copper oxidases. Biochimica Et Biophysica Acta. 1847: 109-18. PMID 24998308 DOI: 10.1016/j.bbabio.2014.06.008  1
2014 Xiang D, Magana D, Dyer RB. CO2 reduction catalyzed by mercaptopteridine on glassy carbon. Journal of the American Chemical Society. 136: 14007-10. PMID 25259884 DOI: 10.1021/ja5081103  1
2014 Reddish MJ, Peng HL, Deng H, Panwar KS, Callender R, Dyer RB. Direct evidence of catalytic heterogeneity in lactate dehydrogenase by temperature jump infrared spectroscopy. The Journal of Physical Chemistry. B. 118: 10854-62. PMID 25149276 DOI: 10.1021/jp5050546  1
2014 Davis CM, Dyer RB. WW domain folding complexity revealed by infrared spectroscopy. Biochemistry. 53: 5476-84. PMID 25121968 DOI: 10.1021/bi500556h  1
2014 Zhao C, Glass EN, Chica B, Musaev DG, Sumliner JM, Dyer RB, Lian T, Hill CL. All-inorganic networks and tetramer based on tin(II)-containing polyoxometalates: tuning structural and spectral properties with lone-pairs. Journal of the American Chemical Society. 136: 12085-91. PMID 25076405 DOI: 10.1021/ja5060127  1
2014 Peng HL, Deng H, Dyer RB, Callender R. Energy landscape of the Michaelis complex of lactate dehydrogenase: relationship to catalytic mechanism. Biochemistry. 53: 1849-57. PMID 24576110 DOI: 10.1021/bi500215a  1
2014 Li G, Magana D, Dyer RB. Anisotropic energy flow and allosteric ligand binding in albumin. Nature Communications. 5: 3100. PMID 24445265 DOI: 10.1038/ncomms4100  1
2014 Zheng W, Liu Y, West A, Schuler EE, Yehl K, Dyer RB, Kindt JT, Salaita K. Quantum dots encapsulated within phospholipid membranes: phase-dependent structure, photostability, and site-selective functionalization. Journal of the American Chemical Society. 136: 1992-9. PMID 24417287 DOI: 10.1021/ja411339f  1
2014 Kise DP, Magana D, Reddish MJ, Dyer RB. Submillisecond mixing in a continuous-flow, microfluidic mixer utilizing mid-infrared hyperspectral imaging detection. Lab On a Chip. 14: 584-91. PMID 24302515 DOI: 10.1039/c3lc51171e  1
2013 Davis CM, Dyer RB. Dynamics of an ultrafast folding subdomain in the context of a larger protein fold. Journal of the American Chemical Society. 135: 19260-7. PMID 24320936 DOI: 10.1021/ja409608r  1
2012 Vu DM, Brewer SH, Dyer RB. Early turn formation and chain collapse drive fast folding of the major cold shock protein CspA of Escherichia coli. Biochemistry. 51: 9104-11. PMID 23098216 DOI: 10.1021/bi301296y  1
2012 Li G, Magana D, Dyer RB. Direct observation and control of ultrafast photoinduced twisted intramolecular charge transfer (TICT) in triphenyl-methane dyes. The Journal of Physical Chemistry. B. 116: 12590-6. PMID 23009668 DOI: 10.1021/jp307091f  1
2012 Yehl K, Joshi JP, Greene BL, Dyer RB, Nahta R, Salaita K. Catalytic deoxyribozyme-modified nanoparticles for RNAi-independent gene regulation Acs Nano. 6: 9150-9157. PMID 22966955 DOI: 10.1021/nn3034265  1
2012 Davis CM, Xiao S, Raleigh DP, Dyer RB. Raising the speed limit for β-hairpin formation. Journal of the American Chemical Society. 134: 14476-82. PMID 22873643 DOI: 10.1021/ja3046734  1
2012 Greene BL, Joseph CA, Maroney MJ, Dyer RB. Direct evidence of active-site reduction and photodriven catalysis in sensitized hydrogenase assemblies. Journal of the American Chemical Society. 134: 11108-11. PMID 22716776 DOI: 10.1021/ja3042367  1
2012 Brewer SH, Tang Y, Vu DM, Gnanakaran S, Raleigh DP, Dyer RB. Temperature dependence of water interactions with the amide carbonyls of α-helices. Biochemistry. 51: 5293-9. PMID 22680405 DOI: 10.1021/bi3006434  1
2012 Li G, Magana D, Dyer RB. Photoinduced electron transfer in folic acid investigated by ultrafast infrared spectroscopy. The Journal of Physical Chemistry. B. 116: 3467-75. PMID 22364409 DOI: 10.1021/jp300392a  1
2011 Nagarajan S, Taskent-Sezgin H, Parul D, Carrico I, Raleigh DP, Dyer RB. Differential ordering of the protein backbone and side chains during protein folding revealed by site-specific recombinant infrared probes. Journal of the American Chemical Society. 133: 20335-40. PMID 22039909 DOI: 10.1021/ja2071362  1
2011 Deng H, Vu DV, Clinch K, Desamero R, Dyer RB, Callender R. Conformational heterogeneity within the Michaelis complex of lactate dehydrogenase. The Journal of Physical Chemistry. B. 115: 7670-8. PMID 21568287 DOI: 10.1021/jp2015929  1
2011 Magana D, Parul D, Dyer RB, Shreve AP. Implementation of time-resolved step-scan fourier transform infrared (FT-IR) spectroscopy using a kHz repetition rate pump laser. Applied Spectroscopy. 65: 535-42. PMID 21513597 DOI: 10.1366/10-06179  1
2010 Taskent-Sezgin H, Chung J, Banerjee PS, Nagarajan S, Dyer RB, Carrico I, Raleigh DP. Azidohomoalanine: a conformationally sensitive IR probe of protein folding, protein structure, and electrostatics. Angewandte Chemie (International Ed. in English). 49: 7473-5. PMID 20815000 DOI: 10.1002/anie.201003325  1
2009 Dyer RB, Brauns EB. Laser-induced temperature jump infrared measurements of RNA folding. Methods in Enzymology. 469: 353-72. PMID 20946798 DOI: 10.1016/S0076-6879(09)69017-0  1
2007 Marecek J, Song B, Brewer S, Belyea J, Dyer RB, Raleigh DP. A simple and economical method for the production of 13C,18O-labeled Fmoc-amino acids with high levels of enrichment: applications to isotope-edited IR studies of proteins. Organic Letters. 9: 4935-7. PMID 17958432 DOI: 10.1021/ol701913p  1
2007 Religa TL, Johnson CM, Vu DM, Brewer SH, Dyer RB, Fersht AR. The helix-turn-helix motif as an ultrafast independently folding domain: The pathway of folding of Engrailed homeodomain Proceedings of the National Academy of Sciences of the United States of America. 104: 9272-9277. PMID 17517666 DOI: 10.1073/pnas.0703434104  1
2007 Brewer SH, Song B, Raleigh DP, Dyer RB. Residue specific resolution of protein folding dynamics using isotope-edited infrared temperature jump spectroscopy. Biochemistry. 46: 3279-85. PMID 17305369 DOI: 10.1021/bi602372y  1
2007 Toepke MW, Brewer SH, Vu DM, Rector KD, Morgan JE, Gennis RB, Kenis PJ, Dyer RB. Microfluidic flow-flash: method for investigating protein dynamics. Analytical Chemistry. 79: 122-8. PMID 17194129 DOI: 10.1021/ac061193x  1
2006 Callender R, Dyer RB. Advances in time-resolved approaches to characterize the dynamical nature of enzymatic catalysis. Chemical Reviews. 106: 3031-42. PMID 16895316 DOI: 10.1021/cr050284b  1
2006 Barry BA, Cooper IB, De Riso A, Brewer SH, Vu DM, Dyer RB. Time-resolved vibrational spectroscopy detects protein-based intermediates in the photosynthetic oxygen-evolving cycle. Proceedings of the National Academy of Sciences of the United States of America. 103: 7288-91. PMID 16632606 DOI: 10.1073/pnas.0600216103  1
2005 Brewer SH, Vu DM, Tang Y, Li Y, Franzen S, Raleigh DP, Dyer RB. Effect of modulating unfolded state structure on the folding kinetics of the villin headpiece subdomain. Proceedings of the National Academy of Sciences of the United States of America. 102: 16662-7. PMID 16269546 DOI: 10.1073/pnas.0505432102  1
2005 Fesinmeyer RM, Peterson ES, Dyer RB, Andersen NH. Studies of helix fraying and solvation using 13C' isotopomers. Protein Science : a Publication of the Protein Society. 14: 2324-32. PMID 16131660 DOI: 10.1110/ps.051510705  1
2005 Brauns EB, Dyer RB. Time-resolved infrared spectroscopy of RNA folding. Biophysical Journal. 89: 3523-30. PMID 16126826 DOI: 10.1529/biophysj.105.061531  1
2005 Dyer RB, Maness SJ, Franzen S, Fesinmeyer RM, Olsen KA, Andersen NH. Hairpin folding dynamics: the cold-denatured state is predisposed for rapid refolding. Biochemistry. 44: 10406-15. PMID 16042418 DOI: 10.1021/bi050698z  1
2005 McClendon S, Vu DM, Clinch K, Callender R, Dyer RB. Structural transformations in the dynamics of Michaelis complex formation in lactate dehydrogenase. Biophysical Journal. 89: L07-9. PMID 15879476 DOI: 10.1529/biophysj.105.064675  1
2004 Dyer RB, Maness SJ, Peterson ES, Franzen S, Fesinmeyer RM, Andersen NH. The mechanism of beta-hairpin formation. Biochemistry. 43: 11560-6. PMID 15350142 DOI: 10.1021/bi049177m  1
2004 Vu DM, Peterson ES, Dyer RB. Experimental resolution of early steps in protein folding: testing molecular dynamics simulations. Journal of the American Chemical Society. 126: 6546-7. PMID 15161270 DOI: 10.1021/ja048416q  1
2004 McMahon BH, Fabian M, Tomson F, Causgrove TP, Bailey JA, Rein FN, Dyer RB, Palmer G, Gennis RB, Woodruff WH. FTIR studies of internal proton transfer reactions linked to inter-heme electron transfer in bovine cytochrome c oxidase. Biochimica Et Biophysica Acta. 1655: 321-31. PMID 15100047 DOI: 10.1016/j.bbabio.2004.01.007  1
2002 Tomson F, Bailey JA, Gennis RB, Unkefer CJ, Li Z, Silks LA, Martinez RA, Donohoe RJ, Dyer RB, Woodruff WH. Direct infrared detection of the covalently ring linked His-Tyr structure in the active site of the heme-copper oxidases. Biochemistry. 41: 14383-90. PMID 12450405 DOI: 10.1021/bi026370c  1
2002 Bailey JA, Tomson FL, Mecklenburg SL, MacDonald GM, Katsonouri A, Puustinen A, Gennis RB, Woodruff WH, Dyer RB. Time-resolved step-scan Fourier transform infrared spectroscopy of the CO adducts of bovine cytochrome c oxidase and of cytochrome bo(3) from Escherichia coli. Biochemistry. 41: 2675-83. PMID 11851414 DOI: 10.1021/bi010823g  1
2001 Franzen S, Bailey J, Dyer RB, Woodruff WH, Hu RB, Thomas MR, Boxer SG. A photolysis-triggered heme ligand switch in H93G myoglobin. Biochemistry. 40: 5299-305. PMID 11318654  1
1998 Callender RH, Dyer RB, Gilmanshin R, Woodruff WH. Fast events in protein folding: the time evolution of primary processes. Annual Review of Physical Chemistry. 49: 173-202. PMID 9933907 DOI: 10.1146/annurev.physchem.49.1.173  1
1998 Kim Y, Babcock GT, Surerus KK, Fee JA, Dyer RB, Woodruff WH, Oertling WA. Cyanide binding and active site structure in heme-copper oxidases: normal coordinate analysis of iron-cyanide vibrations of a3(2+)CN- complexes of cytochromes ba3 and aa3. Biospectroscopy. 4: 1-15. PMID 9547010 DOI: 10.1002/(SICI)1520-6343(1998)4:1<1::AID-BSPY1>3.0.CO;2-A  1
1997 Gilmanshin R, Williams S, Callender RH, Woodruff WH, Dyer RB. Fast events in protein folding: relaxation dynamics and structure of the I form of apomyoglobin. Biochemistry. 36: 15006-12. PMID 9398226 DOI: 10.1021/bi970634r  1
1997 Puustinen A, Bailey JA, Dyer RB, Mecklenburg SL, Wikström M, Woodruff WH. Fourier transform infrared evidence for connectivity between CuB and glutamic acid 286 in cytochrome bo3 from Escherichia coli. Biochemistry. 36: 13195-200. PMID 9341207 DOI: 10.1021/bi971091o  1
1997 Riistama S, Hummer G, Puustinen A, Dyer RB, Woodruff WH, Wikström M. Bound water in the proton translocation mechanism of the haem-copper oxidases. Febs Letters. 414: 275-80. PMID 9315701 DOI: 10.1016/s0014-5793(97)01003-x  1
1997 Gilmanshin R, Williams S, Callender RH, Woodruff WH, Dyer RB. Fast events in protein folding: relaxation dynamics of secondary and tertiary structure in native apomyoglobin. Proceedings of the National Academy of Sciences of the United States of America. 94: 3709-13. PMID 9108042 DOI: 10.1073/pnas.94.8.3709  1
1996 Decatur SM, Franzen S, DePillis GD, Dyer RB, Woodruff WH, Boxer SG. Trans effects in nitric oxide binding to myoglobin cavity mutant H93G. Biochemistry. 35: 4939-44. PMID 8664286 DOI: 10.1021/bi951661p  1
1996 Williams S, Causgrove TP, Gilmanshin R, Fang KS, Callender RH, Woodruff WH, Dyer RB. Fast events in protein folding: helix melting and formation in a small peptide. Biochemistry. 35: 691-7. PMID 8547249 DOI: 10.1021/bi952217p  1
1994 Dyer RB, Peterson KA, Stoutland PO, Woodruff WH. Picosecond infrared study of the photodynamics of carbonmonoxy-cytochrome c oxidase. Biochemistry. 33: 500-7. PMID 8286380 DOI: 10.1021/bi00168a015  1
1994 Oertling WA, Surerus KK, Einarsdóttir O, Fee JA, Dyer RB, Woodruff WH. Spectroscopic characterization of cytochrome ba3, a terminal oxidase from Thermus thermophilus: comparison of the a3/CuB site to that of bovine cytochrome aa3. Biochemistry. 33: 3128-41. PMID 8130228 DOI: 10.1021/bi00176a048  1
1993 Einarsdóttir O, Dyer RB, Lemon DD, Killough PM, Hubig SM, Atherton SJ, López-Garriga JJ, Palmer G, Woodruff WH. Photodissociation and recombination of carbonmonoxy cytochrome oxidase: Dynamics from picoseconds to kiloseconds Biochemistry. 32: 12013-12024. PMID 8218278  1
1992 Stoutland PO, Dyer RB, Woodruff WH. Ultrafast infrared spectroscopy. Science (New York, N.Y.). 257: 1913-7. PMID 1329200 DOI: 10.1126/science.1329200  1
1992 Surerus KK, Oertling WA, Fan C, Gurbiel RJ, Einarsdóttir O, Antholine WE, Dyer RB, Hoffman BM, Woodruff WH, Fee JA. Reaction of cyanide with cytochrome ba3 from Thermus thermophilus: spectroscopic characterization of the Fe(II)a3-CN.Cu(II)B-CN complex suggests four 14N atoms are coordinated to CuB. Proceedings of the National Academy of Sciences of the United States of America. 89: 3195-9. PMID 1314380 DOI: 10.1073/pnas.89.8.3195  1
1992 Kuila D, Schoonover JR, Dyer RB, Batie CJ, Ballou DP, Fee JA, Woodruff WH. Resonance Raman studies of Rieske-type proteins. Biochimica Et Biophysica Acta. 1140: 175-83. PMID 1280165 DOI: 10.1016/0005-2728(92)90007-O  1
1991 Woodruff WH, Einarsdóttir O, Dyer RB, Bagley KA, Palmer G, Atherton SJ, Goldbeck RA, Dawes TD, Kliger DS. Nature and functional implications of the cytochrome a3 transients after photodissociation of CO-cytochrome oxidase. Proceedings of the National Academy of Sciences of the United States of America. 88: 2588-92. PMID 1848709  0.24
1988 Schoonover JR, Dyer RB, Woodruff WH, Baker GM, Noguchi M, Palmer G. A comparison of the resonance Raman properties of the fast and slow forms of cytochrome oxidase Biochemistry. 27: 5433-5440. PMID 2846036  1
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