| Year |
Citation |
Score |
| 2013 |
Kaya H, Uzunoğlu Z, Chan HS. Spatial ranges of driving forces are a key determinant of protein folding cooperativity and rate diversity. Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics. 88: 044701. PMID 24229309 DOI: 10.1103/PhysRevE.88.044701 |
0.704 |
|
| 2012 |
Kaya H, Uzunoglu Z. Energetics of Protein Folding Kinetics Biophysical Journal. 102: 58a. DOI: 10.1016/J.BPJ.2011.11.345 |
0.603 |
|
| 2010 |
Kaya H, Berezovsky IN. Negative and Positive Design in Protein Folding and Thermodynamic Stability: Insights from Computational Mutagenesis and Simulations Biophysical Journal. 98: 637a. DOI: 10.1016/J.BPJ.2009.12.3488 |
0.38 |
|
| 2005 |
Kaya H, Liu Z, Chan HS. Chevron behavior and isostable enthalpic barriers in protein folding: successes and limitations of simple Gō-like modeling. Biophysical Journal. 89: 520-35. PMID 15863486 DOI: 10.1529/Biophysj.104.057471 |
0.761 |
|
| 2005 |
Kaya H, Chan HS. Explicit-chain model of native-state hydrogen exchange: implications for event ordering and cooperativity in protein folding. Proteins. 58: 31-44. PMID 15468168 DOI: 10.1002/prot.20286 |
0.722 |
|
| 2004 |
Ollerenshaw JE, Kaya H, Chan HS, Kay LE. Sparsely populated folding intermediates of the Fyn SH3 domain: matching native-centric essential dynamics and experiment. Proceedings of the National Academy of Sciences of the United States of America. 101: 14748-53. PMID 15469926 DOI: 10.1073/Pnas.0404436101 |
0.737 |
|
| 2004 |
Chan HS, Shimizu S, Kaya H. Cooperativity principles in protein folding. Methods in Enzymology. 380: 350-79. PMID 15051345 DOI: 10.1016/S0076-6879(04)80016-8 |
0.725 |
|
| 2004 |
Kaya H, Chan HS. Corrigendum to: “Solvation Effects and Driving Forces for Protein Thermodynamic and Kinetic Cooperativity: How Adequate is Native-Centric Topological Modeling?” [J. Mol. Biol. (2003) 326, 911–931] Journal of Molecular Biology. 337: 1069-1070. DOI: 10.1016/J.JMB.2004.02.025 |
0.658 |
|
| 2003 |
Kaya H, Chan HS. Contact order dependent protein folding rates: kinetic consequences of a cooperative interplay between favorable nonlocal interactions and local conformational preferences. Proteins. 52: 524-33. PMID 12910452 DOI: 10.1002/prot.10478 |
0.722 |
|
| 2003 |
Kaya H, Chan HS. Simple two-state protein folding kinetics requires near-levinthal thermodynamic cooperativity. Proteins. 52: 510-23. PMID 12910451 DOI: 10.1002/prot.10506 |
0.777 |
|
| 2003 |
Kaya H, Chan HS. Origins of chevron rollovers in non-two-state protein folding kinetics. Physical Review Letters. 90: 258104. PMID 12857173 DOI: 10.1103/PhysRevLett.90.258104 |
0.76 |
|
| 2003 |
Kaya H, Chan HS. Solvation effects and driving forces for protein thermodynamic and kinetic cooperativity: how adequate is native-centric topological modeling? Journal of Molecular Biology. 326: 911-31. PMID 12581650 |
0.775 |
|
| 2002 |
Kaya H, Chan HS. Towards a consistent modeling of protein thermodynamic and kinetic cooperativity: how applicable is the transition state picture to folding and unfolding? Journal of Molecular Biology. 315: 899-909. PMID 11812156 DOI: 10.1006/jmbi.2001.5266 |
0.767 |
|
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