Year |
Citation |
Score |
2023 |
Stecher K, Krieger F, Schleeger M, Kiefhaber T. Local and Large-Scale Conformational Dynamics in Unfolded Proteins and IDPs. I. Effect of Solvent Viscosity and Macromolecular Crowding. The Journal of Physical Chemistry. B. 127: 8095-8105. PMID 37722681 DOI: 10.1021/acs.jpcb.3c04070 |
0.305 |
|
2023 |
Krieger F, Stecher K, Nyffenegger C, Schleeger M, Kiefhaber T. Local and Large-Scale Conformational Dynamics in Unfolded Proteins and IDPs. II. Effect of Temperature and Internal Friction. The Journal of Physical Chemistry. B. 127: 8106-8115. PMID 37722680 DOI: 10.1021/acs.jpcb.3c04072 |
0.407 |
|
2014 |
Neumaier S, Kiefhaber T. Redefining the dry molten globule state of proteins Journal of Molecular Biology. 426: 2520-2528. PMID 24792909 DOI: 10.1016/J.Jmb.2014.04.022 |
0.418 |
|
2013 |
Neumaier S, Büttner M, Bachmann A, Kiefhaber T. Transition state and ground state properties of the helix-coil transition in peptides deduced from high-pressure studies. Proceedings of the National Academy of Sciences of the United States of America. 110: 20988-93. PMID 24324160 DOI: 10.1073/Pnas.1317973110 |
0.471 |
|
2013 |
Neumaier S, Reiner A, Büttner M, Fierz B, Kiefhaber T. Testing the diffusing boundary model for the helix-coil transition in peptides. Proceedings of the National Academy of Sciences of the United States of America. 110: 12905-10. PMID 23878243 DOI: 10.1073/Pnas.1303515110 |
0.744 |
|
2012 |
Kiefhaber T, Bachmann A, Jensen KS. Dynamics and mechanisms of coupled protein folding and binding reactions Current Opinion in Structural Biology. 22: 21-29. PMID 22129832 DOI: 10.1016/j.sbi.2011.09.010 |
0.31 |
|
2011 |
Bachmann A, Wildemann D, Praetorius F, Fischer G, Kiefhaber T. Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction Proceedings of the National Academy of Sciences of the United States of America. 108: 3952-3957. PMID 21325613 DOI: 10.1073/Pnas.1012668108 |
0.649 |
|
2011 |
Reiner A, Fierz B, Kiefhaber T. Conformational dynamics in peptides and proteins studied by triplet-triplet energy transfer Methods in Protein Biochemistry. 73-94. DOI: 10.1515/9783110252361 |
0.729 |
|
2010 |
Reiner A, Henklein P, Kiefhaber T. An unlocking/relocking barrier in conformational fluctuations of villin headpiece subdomain. Proceedings of the National Academy of Sciences of the United States of America. 107: 4955-60. PMID 20194774 DOI: 10.1073/Pnas.0910001107 |
0.685 |
|
2009 |
Habazettl J, Reiner A, Kiefhaber T. NMR structure of a monomeric intermediate on the evolutionarily optimized assembly pathway of a small trimerization domain. Journal of Molecular Biology. 389: 103-14. PMID 19361528 DOI: 10.1016/J.Jmb.2009.03.073 |
0.657 |
|
2009 |
Fierz B, Reiner A, Kiefhaber T. Local conformational dynamics in alpha-helices measured by fast triplet transfer. Proceedings of the National Academy of Sciences of the United States of America. 106: 1057-62. PMID 19131517 DOI: 10.1073/Pnas.0808581106 |
0.755 |
|
2008 |
Reiner A, Wildemann D, Fischer G, Kiefhaber T. Effect of thioxopeptide bonds on alpha-helix structure and stability. Journal of the American Chemical Society. 130: 8079-84. PMID 18512914 DOI: 10.1021/Ja8015044 |
0.688 |
|
2008 |
Schlepckow K, Wirmer J, Bachmann A, Kiefhaber T, Schwalbe H. Conserved Folding Pathways of α-Lactalbumin and Lysozyme Revealed by Kinetic CD, Fluorescence, NMR, and Interrupted Refolding Experiments Journal of Molecular Biology. 378: 686-698. PMID 18377934 DOI: 10.1016/J.Jmb.2008.02.033 |
0.475 |
|
2008 |
Möglich A, Joder K, Kiefhaber T. End-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formation (Proceedings of the National Academy of Sciences of the United States of America (2006) 103, (12394-12399) 10.1073/pnas.0604748103) Proceedings of the National Academy of Sciences of the United States of America. 105: 6787. DOI: 10.1073/pnas.0803144105 |
0.635 |
|
2008 |
Fierz B, Kiefhaber T. Dynamics of Unfolded Polypeptide Chains Protein Folding Handbook. 2: 809-855. DOI: 10.1002/9783527619498.ch22 |
0.63 |
|
2008 |
Kiefhaber T, Sánchez IE, Bachmann A. Characterization of Protein Folding Barriers with Rate Equilibrium Free Energy Relationships Protein Folding Handbook. 1: 411-444. DOI: 10.1002/9783527619498.ch12b |
0.636 |
|
2008 |
Bachmann A, Kiefhaber T. Kinetic Mechanisms in Protein Folding Protein Folding Handbook. 1: 377-410. DOI: 10.1002/9783527619498.ch12a |
0.374 |
|
2008 |
Buchner J, Kiefhaber T. Protein Folding Handbook Protein Folding Handbook. 1: 1-1333. DOI: 10.1002/9783527619498 |
0.561 |
|
2007 |
Wildemann D, Schiene-Fischer C, Aumüller T, Bachmann A, Kiefhaber T, Lücke C, Fischer G. A nearly isosteric photosensitive amide-backbone substitution allows enzyme activity switching in ribonuclease S Journal of the American Chemical Society. 129: 4910-4918. PMID 17397159 DOI: 10.1021/Ja069048O |
0.569 |
|
2007 |
Fierz B, Satzger H, Root C, Gilch P, Zinth W, Kiefhaber T. Loop formation in unfolded polypeptide chains on the picoseconds to microseconds time scale. Proceedings of the National Academy of Sciences of the United States of America. 104: 2163-8. PMID 17284588 DOI: 10.1073/Pnas.0611087104 |
0.714 |
|
2007 |
Fierz B, Kiefhaber T. End-to-end vs interior loop formation kinetics in unfolded polypeptide chains. Journal of the American Chemical Society. 129: 672-9. PMID 17227031 DOI: 10.1021/Ja0666396 |
0.682 |
|
2007 |
Fierz B, Joder K, Krieger F, Kiefhaber T. Using triplet-triplet energy transfer to measure conformational dynamics in polypeptide chains. Methods in Molecular Biology (Clifton, N.J.). 350: 169-87. PMID 16957323 DOI: 10.1385/1-59745-189-4:169 |
0.685 |
|
2006 |
Möglich A, Joder K, Kiefhaber T. End-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formation. Proceedings of the National Academy of Sciences of the United States of America. 103: 12394-9. PMID 16894178 DOI: 10.1073/Pnas.0604748103 |
0.706 |
|
2006 |
Heinz B, Schmidt B, Root C, Satzger H, Milota F, Fierz B, Kiefhaber T, Zinth W, Gilch P. On the unusual fluorescence properties of xanthone in water. Physical Chemistry Chemical Physics : Pccp. 8: 3432-9. PMID 16855722 DOI: 10.1039/B603560D |
0.63 |
|
2006 |
Schätzle M, Kiefhaber T. Shape of the free energy barriers for protein folding probed by multiple perturbation analysis Journal of Molecular Biology. 357: 655-664. PMID 16442561 DOI: 10.1016/J.Jmb.2005.12.081 |
0.464 |
|
2006 |
Heinz B, Schmidt B, Root C, Satzger H, Milota F, Fierz B, Kiefhaber T, Zinth W, Gilch P. Slow fluorescence and fast intersystem crossing - the xanthone anomaly Optics Infobase Conference Papers. |
0.565 |
|
2005 |
Bachmann A, Kiefhaber T, Boudko S, Engel J, Bächinger HP. Collagen triple-helix formation in all-trans chains proceeds by a nucleation/growth mechanism with a purely entropic barrier Proceedings of the National Academy of Sciences of the United States of America. 102: 13897-13902. PMID 16172389 DOI: 10.1073/Pnas.0505141102 |
0.52 |
|
2005 |
Bodenreider C, Kiefhaber T. Interpretation of protein folding ψ values Journal of Molecular Biology. 351: 393-401. PMID 16005895 DOI: 10.1016/J.Jmb.2005.05.062 |
0.486 |
|
2005 |
Krieger F, Möglich A, Kiefhaber T. Effect of proline and glycine residues on dynamics and barriers of loop formation in polypeptide chains Journal of the American Chemical Society. 127: 3346-3352. PMID 15755151 DOI: 10.1021/Ja042798I |
0.72 |
|
2005 |
Möglich A, Krieger F, Kiefhaber T. Molecular basis for the effect of urea and guanidinium chloride on the dynamics of unfolded polypeptide chains Journal of Molecular Biology. 345: 153-162. PMID 15567418 DOI: 10.1016/J.Jmb.2004.10.036 |
0.717 |
|
2004 |
Meier S, Güthe S, Kiefhaber T, Grzesiek S. Foldon, the natural trimerization domain of T4 fibritin, dissociates into a monomeric A-state form containing a stable β-hairpin: Atomic details of trimer dissociation and local β-hairpin stability from residual dipolar couplings Journal of Molecular Biology. 344: 1051-1069. PMID 15544812 DOI: 10.1016/J.Jmb.2004.09.079 |
0.458 |
|
2004 |
Sánchez IE, Morillas M, Zobeley E, Kiefhaber T, Glockshuber R. Fast folding of the two-domain semliki forest virus capsid protein explains co-translational proteolytic activity. Journal of Molecular Biology. 338: 159-67. PMID 15050831 DOI: 10.1016/J.Jmb.2004.02.037 |
0.67 |
|
2004 |
Güthe S, Kapinos L, Möglich A, Meier S, Grzesiek S, Kiefhaber T. Very fast folding and association of a trimerization domain from bacteriophage T4 fibritin Journal of Molecular Biology. 337: 905-915. PMID 15033360 DOI: 10.1016/J.Jmb.2004.02.020 |
0.732 |
|
2004 |
Satzger H, Schmidt B, Root C, Zinth W, Fierz B, Krieger F, Kiefhaber T, Gilch P. Ultrafast quenching of the xanthone triplet by energy transfer: New insight into the intersystem crossing kinetics Journal of Physical Chemistry A. 108: 10072-10079. DOI: 10.1021/Jp047583+ |
0.666 |
|
2004 |
Krieger F, Fierz B, Axthelm F, Joder K, Meyer D, Kiefhaber T. Intrachain diffusion in a protein loop fragment from carp parvalbumin Chemical Physics. 307: 209-215. DOI: 10.1016/J.Chemphys.2004.05.036 |
0.729 |
|
2003 |
Sánchez IE, Kiefhaber T. Origin of unusual phi-values in protein folding: evidence against specific nucleation sites. Journal of Molecular Biology. 334: 1077-85. PMID 14643667 DOI: 10.1016/J.Jmb.2003.10.016 |
0.653 |
|
2003 |
Krieger F, Fierz B, Bieri O, Drewello M, Kiefhaber T. Dynamics of unfolded polypeptide chains as model for the earliest steps in protein folding. Journal of Molecular Biology. 332: 265-74. PMID 12946363 DOI: 10.1016/S0022-2836(03)00892-1 |
0.736 |
|
2003 |
Sánchez IE, Kiefhaber T. Hammond behavior versus ground state effects in protein folding: evidence for narrow free energy barriers and residual structure in unfolded states. Journal of Molecular Biology. 327: 867-84. PMID 12654269 DOI: 10.1016/S0022-2836(03)00171-2 |
0.697 |
|
2003 |
Sánchez IE, Kiefhaber T. Non-linear rate-equilibrium free energy relationships and Hammond behavior in protein folding. Biophysical Chemistry. 100: 397-407. PMID 12646379 DOI: 10.1016/S0301-4622(02)00294-6 |
0.659 |
|
2003 |
Pappenberger G, Bachmann A, Müller R, Aygün H, Engels JW, Kiefhaber T. Kinetic mechanism and catalysis of a native-state prolyl isomerization reaction Journal of Molecular Biology. 326: 235-246. PMID 12547205 DOI: 10.1016/S0022-2836(02)01373-6 |
0.485 |
|
2003 |
Sánchez IE, Kiefhaber T. Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding. Journal of Molecular Biology. 325: 367-76. PMID 12488101 DOI: 10.1016/S0022-2836(02)01230-5 |
0.709 |
|
2002 |
Bachmann A, Segel D, Kiefhaber T. Test for cooperativity in the early kinetic intermediate in lysozyme folding Biophysical Chemistry. 96: 141-151. PMID 12034436 DOI: 10.1016/S0301-4622(02)00020-0 |
0.501 |
|
2001 |
Bieri O, Kiefhaber T. Origin of apparent fast and non-exponential kinetics of lysozyme folding measured in pulsed hydrogen exchange experiments Journal of Molecular Biology. 310: 919-935. PMID 11453698 DOI: 10.1006/Jmbi.2001.4804 |
0.466 |
|
2001 |
Pappenberger G, Aygün H, Engels JW, Reimer U, Fischer G, Kiefhaber T. Nonprolyl cis peptide bonds in unfolded proteins cause complex folding kinetics Nature Structural Biology. 8: 452-458. PMID 11323723 DOI: 10.1038/87624 |
0.647 |
|
2001 |
Bachmann A, Kiefhaber T. Apparent two-state tendamistat folding is a sequential process along a defined route Journal of Molecular Biology. 306: 375-386. PMID 11237606 DOI: 10.1006/Jmbi.2000.4399 |
0.52 |
|
2000 |
Pappenberger G, Saudan C, Becker M, Merbach AE, Kiefhaber T. Denaturant-induced movement of the transition state of protein folding revealed by high-pressure stopped-flow measurements Proceedings of the National Academy of Sciences of the United States of America. 97: 17-22. PMID 10618363 DOI: 10.1073/Pnas.97.1.17 |
0.416 |
|
1999 |
Bieri O, Kiefhaber T. Elementary steps in protein folding Biological Chemistry. 380: 923-929. PMID 10494843 DOI: 10.1515/Bc.1999.114 |
0.474 |
|
1999 |
Bieri O, Wildegger G, Bachmann A, Wagner C, Kiefhaber T. A salt-induced kinetic intermediate is on a new parallel pathway of lysozyme folding Biochemistry. 38: 12460-12470. PMID 10493816 DOI: 10.1021/Bi9909703 |
0.477 |
|
1999 |
Bieri O, Wirz J, Hellrung B, Schutkowski M, Drewello M, Kiefhaber T. The speed limit for protein folding measured by triplet-triplet energy transfer Proceedings of the National Academy of Sciences of the United States of America. 96: 9597-9601. PMID 10449738 DOI: 10.1073/Pnas.96.17.9597 |
0.502 |
|
1999 |
Wagner C, Kiefhaber T. Intermediates can accelerate protein folding Proceedings of the National Academy of Sciences of the United States of America. 96: 6716-6721. PMID 10359778 DOI: 10.1073/Pnas.96.12.6716 |
0.482 |
|
1999 |
Segel DJ, Bachmann A, Hofrichter J, Hodgson KO, Doniach S, Kiefhaber T. Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering. Journal of Molecular Biology. 288: 489-99. PMID 10329156 DOI: 10.1006/Jmbi.1999.2703 |
0.484 |
|
1998 |
Phale PS, Philippsen A, Kiefhaber T, Koebnik R, Phale VP, Schirmer T, Rosenbusch JP. Stability of trimeric OmpF porin: The contributions of the latching loop L2 Biochemistry. 37: 15663-15670. PMID 9843370 DOI: 10.1021/Bi981215C |
0.359 |
|
1998 |
Chen L, Wildegger G, Kiefhaber T, Hodgson KO, Doniach S. Kinetics of lysozyme refolding: structural characterization of a non-specifically collapsed state using time-resolved X-ray scattering. Journal of Molecular Biology. 276: 225-37. PMID 9514723 DOI: 10.1006/Jmbi.1997.1514 |
0.439 |
|
1997 |
Wildegger G, Kiefhaber T. Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate Journal of Molecular Biology. 270: 294-304. PMID 9236130 DOI: 10.1006/Jmbi.1997.1030 |
0.512 |
|
1997 |
Schönbrunner N, Pappenberger G, Scharf M, Engels J, Kiefhaber T. Effect of preformed correct tertiary interactions on rapid two-state tendamistat folding: Evidence for hairpins as initiation sites for β-sheet formation Biochemistry. 36: 9057-9065. PMID 9220995 DOI: 10.1021/Bi970594R |
0.412 |
|
1997 |
Schönbrunner N, Koller KP, Kiefhaber T. Folding of the disulfide-bonded β-sheet protein tendamistat: Rapid two-state folding without hydrophobic collapse Journal of Molecular Biology. 268: 526-538. PMID 9159488 DOI: 10.1006/Jmbi.1997.0960 |
0.55 |
|
1997 |
Kiefhaber T, Bachmann A, Wildegger G, Wagner C. Direct measurement of nucleation and growth rates in lysozyme folding Biochemistry. 36: 5108-5112. PMID 9136870 DOI: 10.1021/Bi9702391 |
0.439 |
|
1996 |
Schönbrunner N, Josef W, Engels J, Georg H, Kiefhaber T. Native-like β-structure in a trifluoroethanol-induced partially folded state of the all-β-sheet protein tendamistat Journal of Molecular Biology. 260: 432-445. PMID 8757805 DOI: 10.1006/jmbi.1996.0412 |
0.362 |
|
1996 |
Loh SN, Rohl CA, Kiefhaber T, Baldwin RL. A general two-process model describes the hydrogen exchange behavior of RNase A in unfolding conditions. Proceedings of the National Academy of Sciences of the United States of America. 93: 1982-7. PMID 8700871 DOI: 10.1073/Pnas.93.5.1982 |
0.677 |
|
1996 |
Kiefhaber T, Baldwin RL. Hydrogen exchange and the unfolding pathway of ribonuclease A. Biophysical Chemistry. 59: 351-6. PMID 8672722 DOI: 10.1016/0301-4622(95)00142-5 |
0.684 |
|
1996 |
Berchtold H, Rudolph R, Kiefhaber T, Darlison MG, Breitenbach U, Lübbert H, Boddeke HGWM, Blohm D. Biochemie und Molekulargenetik 1995 Nachrichten Aus Chemie Technik Und Laboratorium. 44: 168-182. DOI: 10.1002/Nadc.19960440209 |
0.445 |
|
1995 |
Kiefhaber T, Labhardt AM, Baldwin RL. Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A. Nature. 375: 513-5. PMID 7777063 DOI: 10.1038/375513A0 |
0.701 |
|
1995 |
Kiefhaber T, Baldwin RL. Kinetics of hydrogen bond breakage in the process of unfolding of ribonuclease A measured by pulsed hydrogen exchange. Proceedings of the National Academy of Sciences of the United States of America. 92: 2657-61. PMID 7708700 DOI: 10.1073/Pnas.92.7.2657 |
0.666 |
|
1995 |
Kiefhaber T, Baldwin RL. Intrinsic stability of individual alpha helices modulates structure and stability of the apomyoglobin molten globule form. Journal of Molecular Biology. 252: 122-32. PMID 7666424 DOI: 10.1006/Jmbi.1995.0479 |
0.69 |
|
1995 |
Kiefhaber T. Protein folding kinetics. Methods in Molecular Biology (Clifton, N.J.). 40: 313-341. PMID 7633528 DOI: 10.1385/0-89603-301-5:313 |
0.488 |
|
1995 |
Kiefhaber T. Kinetic traps in lysozyme folding Proceedings of the National Academy of Sciences of the United States of America. 92: 9029-9033. PMID 7568066 DOI: 10.1073/Pnas.92.20.9029 |
0.498 |
|
1992 |
Kiefhaber T, Grunert HP, Hahn U, Schmid FX. Folding of RNase T1 is decelerated by a specific tertiary contact in a folding intermediate Proteins: Structure, Function and Genetics. 12: 171-179. PMID 1603806 DOI: 10.1002/Prot.340120210 |
0.744 |
|
1992 |
Kiefhaber T, Schmid FX. Kinetic coupling between protein folding and prolyl isomerization. II. Folding of ribonuclease A and ribonuclease T1 Journal of Molecular Biology. 224: 231-240. PMID 1548701 DOI: 10.1016/0022-2836(92)90586-9 |
0.707 |
|
1992 |
Kiefhaber T, Kohler HH, Schmid FX. Kinetic coupling between protein folding and prolyl isomerization. I. Theoretical models Journal of Molecular Biology. 224: 217-229. PMID 1548700 DOI: 10.1016/0022-2836(92)90585-8 |
0.728 |
|
1992 |
Kiefhaber T, Schmid FX, Willaert K, Engelborghs Y, Chaffotte A. Structure of a rapidly formed intermediate in ribonuclease T1 folding Protein Science. 1: 1162-1172. PMID 1304394 DOI: 10.1002/Pro.5560010910 |
0.762 |
|
1992 |
Rudolph R, Siebendritt R, Kiefhaber T. Reversible unfolding and refolding behavior of a monomeric aldolase from Staphylococcus aureus Protein Science. 1: 654-666. PMID 1304364 DOI: 10.1002/Pro.5560010511 |
0.671 |
|
1991 |
Buchner J, Schmidt M, Fuchs M, Jaenicke R, Rudolph R, Schmid FX, Kiefhaber T. GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry. 30: 1586-91. PMID 1671555 DOI: 10.1021/Bi00220A020 |
0.792 |
|
1991 |
Kiefhaber T, Rudolph R, Kohler HH, Buchner J. Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation. Bio/Technology (Nature Publishing Company). 9: 825-9. PMID 1367356 DOI: 10.1038/Nbt0991-825 |
0.688 |
|
1990 |
Buchner J, Kiefhaber T. Folding pathway enigma. Nature. 343: 601-2. PMID 2304534 DOI: 10.1038/343601B0 |
0.479 |
|
1990 |
Kiefhaber T, Schmid FX, Renner M, Hinz HJ, Hahn U, Quaas R. Stability of recombinant Lys25-ribonuclease T1. Biochemistry. 29: 8250-7. PMID 2123715 DOI: 10.1021/Bi00488A008 |
0.693 |
|
1990 |
Kiefhaber T, Grunert HP, Hahn U, Schmid FX. Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding. Biochemistry. 29: 6475-80. PMID 2119802 DOI: 10.1021/Bi00479A020 |
0.688 |
|
1990 |
Kiefhaber T, Quaas R, Hahn U, Schmid FX. Folding of ribonuclease T1. 2. Kinetic models for the folding and unfolding reactions. Biochemistry. 29: 3061-70. PMID 2110824 DOI: 10.1021/Bi00464A024 |
0.731 |
|
1990 |
Kiefhaber T, Quaas R, Hahn U, Schmid FX. Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization. Biochemistry. 29: 3053-61. PMID 2110823 DOI: 10.1021/Bi00464A023 |
0.73 |
|
1989 |
Fischer G, Wittmann-Liebold B, Lang K, Kiefhaber T, Schmid FX. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature. 337: 476-8. PMID 2492638 DOI: 10.1038/337476A0 |
0.747 |
|
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