Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
1R01GM052126-01A2
Application #
2191045
Study Section
Special Emphasis Panel (ZRG3-BBCA (01))
Project Start
1995-09-01
Project End
2000-07-31
Budget Start
1996-08-01
Budget End
1997-07-31
Support Year
1
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Harvard University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
071723621
City
Cambridge
State
MA
Country
United States
Zip Code
02138
Huang, Lei; Shakhnovich, Eugene I (2012) Is there an en route folding intermediate for Cold shock proteins? Protein Sci 21:677-85
Xu, Jiabin; Huang, Lei; Shakhnovich, Eugene I (2011) The ensemble folding kinetics of the FBP28 WW domain revealed by an all-atom Monte Carlo simulation in a knowledge-based potential. Proteins 79:1704-14
Nivon, Lucas G; Shakhnovich, Eugene I (2011) Thermodynamics and kinetics of the hairpin ribozyme from atomistic folding/unfolding simulations. J Mol Biol 411:1128-44
Kutchukian, Peter S; Yang, Jae Shick; Verdine, Gregory L et al. (2009) All-atom model for stabilization of alpha-helical structure in peptides by hydrocarbon staples. J Am Chem Soc 131:4622-7
Lukatsky, D B; Shakhnovich, B E; Mintseris, J et al. (2007) Structural similarity enhances interaction propensity of proteins. J Mol Biol 365:1596-606
Wallin, Stefan; Zeldovich, Konstantin B; Shakhnovich, Eugene I (2007) The folding mechanics of a knotted protein. J Mol Biol 368:884-93
Lam, A R; Borreguero, J M; Ding, F et al. (2007) Parallel folding pathways in the SH3 domain protein. J Mol Biol 373:1348-60
Shakhnovich, Eugene (2006) Protein folding thermodynamics and dynamics: where physics, chemistry, and biology meet. Chem Rev 106:1559-88
Ding, Feng; Guo, Weihua; Dokholyan, Nikolay V et al. (2005) Reconstruction of the src-SH3 protein domain transition state ensemble using multiscale molecular dynamics simulations. J Mol Biol 350:1035-50
Mirny, L A; Shakhnovich, E I (1999) Universally conserved positions in protein folds: reading evolutionary signals about stability, folding kinetics and function. J Mol Biol 291:177-96