scholarly journals Prediction of Native-State Hydrogen Exchange from Perfectly Funneled Energy Landscapes

2011 ◽  
Vol 133 (43) ◽  
pp. 17463-17472 ◽  
Author(s):  
Patricio O. Craig ◽  
Joachim Lätzer ◽  
Patrick Weinkam ◽  
Ryan M. B. Hoffman ◽  
Diego U. Ferreiro ◽  
...  
Biochemistry ◽  
2002 ◽  
Vol 41 (25) ◽  
pp. 7998-8003 ◽  
Author(s):  
Ruiai Chu ◽  
Wuhong Pei ◽  
Jiro Takei ◽  
Yawen Bai

2010 ◽  
Vol 132 (23) ◽  
pp. 8010-8019 ◽  
Author(s):  
Joshua A. Boyer ◽  
Cristina J. Clay ◽  
K. Scott Luce ◽  
Marshall H. Edgell ◽  
Andrew L. Lee

Science ◽  
1995 ◽  
Vol 269 (5221) ◽  
pp. 192-197 ◽  
Author(s):  
Y Bai ◽  
T. Sosnick ◽  
L Mayne ◽  
S. Englander

2004 ◽  
Vol 18 (04) ◽  
pp. 163-172 ◽  
Author(s):  
HU CHEN ◽  
XIN ZHOU ◽  
CHIH YOUNG LIAW ◽  
CHAN GHEE KOH

Based on two-dimensional square lattice models of proteins, the relation between folding time and temperature is studied by Monte Carlo simulation. The results can be represented by a kinetic model with three states — random coil, molten globule, and native state. The folding process is composed of nonspecific collapse and final searching for the native state. At high temperature, it is easy to escape from local traps in the folding process. With decreasing temperature, because of the trapping in local traps, the final searching speed decreases. Then the folding shows chevron rollover. Through the analysis of the fitted parameters of the kinetic model, it is found that the main difference between the energy landscapes of the HP model and the Go model is that the number of local minima of the Go model is less than that of the HP model.


1983 ◽  
Vol 16 (4) ◽  
pp. 521-655 ◽  
Author(s):  
S. Walter Englander ◽  
Neville R. Kallenbach

Though the structures presented in crystallographic models of macromolecules appear to possess rock-like solidity, real proteins and nucleic acids are not particularly rigid. Most structural work to date has centred upon the native state of macromolecules, the most probable macromolecular form. But the native state of a molecule is merely its most abundant form, certainly not its only form. Thermodynamics requires that all other possible structural forms, however improbable, must also exist, albeit with representation corresponding to the factor exp( — Gi/RT) for each state of free energy Gi (see Moelwyn-Hughes, 1961), and one appreciates that each molecule within a population of molecules will in time explore the vast ensemble of possible structural states.


2002 ◽  
Vol 99 (19) ◽  
pp. 12173-12178 ◽  
Author(s):  
L. Hoang ◽  
S. Bedard ◽  
M. M. G. Krishna ◽  
Y. Lin ◽  
S. W. Englander

Biochemistry ◽  
1997 ◽  
Vol 36 (29) ◽  
pp. 8686-8691 ◽  
Author(s):  
Cammon B. Arrington ◽  
Andrew D. Robertson

Sign in / Sign up

Export Citation Format

Share Document