NMR Analysis of Native-State Protein Conformational Flexibility by Hydrogen Exchange

Author(s):  
Griselda Hernández ◽  
David M. LeMaster
Biochemistry ◽  
2002 ◽  
Vol 41 (25) ◽  
pp. 7998-8003 ◽  
Author(s):  
Ruiai Chu ◽  
Wuhong Pei ◽  
Jiro Takei ◽  
Yawen Bai

1995 ◽  
Vol 36 (35) ◽  
pp. 6329-6332 ◽  
Author(s):  
Juan-Félix Espinosa ◽  
Manuel Martín-Pastor ◽  
Juan L. Asensio ◽  
Hansjörg Dietrich ◽  
Manuel Martín-Lomas ◽  
...  

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

2008 ◽  
Vol 9 (2) ◽  
pp. 290-301 ◽  
Author(s):  
Victor A. Jaravine ◽  
Klara Rathgeb-Szabo ◽  
Andrei T. Alexandrescu

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

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