scholarly journals Picosecond to nanosecond dynamics provide a source of conformational entropy for protein folding

2016 ◽  
Vol 18 (31) ◽  
pp. 21527-21538 ◽  
Author(s):  
Andreas M. Stadler ◽  
Franz Demmel ◽  
Jacques Ollivier ◽  
Tilo Seydel
Keyword(s):  
Protein Folding ◽  
Stable Equilibrium ◽  
Conformational Entropy ◽  
Equilibrium Conditions ◽  
Molten Globules ◽  
Nanosecond Dynamics ◽  
Folded Structures

Myoglobin can be trapped in fully folded structures, partially folded molten globules, and unfolded states under stable equilibrium conditions.

scholarly journals Characterization of the dynamics and the conformational entropy in the binding between TAZ1 and CTAD-HIF-1α

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Ida Nyqvist ◽  
Jakob Dogan
Keyword(s):  
Entropy Change ◽  
Side Chain ◽  
Transactivation Domain ◽  
Creb Binding Protein ◽  
Conformational Entropy ◽  
Internal Motions ◽  
Relaxation Measurements ◽  
Nanosecond Dynamics

Abstract The interaction between the C-terminal transactivation domain of HIF-1α (CTAD-HIF-1α) and the transcriptional adapter zinc binding 1 (TAZ1) domain of CREB binding protein participate in the initiation of gene transcription during hypoxia. Unbound CTAD-HIF-1α is disordered but undergoes a disorder-to-order transition upon binding to TAZ1. We have here performed NMR side chain and backbone relaxation studies on TAZ1 and side chain relaxation measurements on CTAD-HIF-1α in order to investigate the role of picosecond to nanosecond dynamics. We find that the internal motions are significantly affected upon binding, both on the side chain and the backbone level. The dynamic response corresponds to a conformational entropy change that contributes substantially to the binding thermodynamics for both binding partners. Furthermore, the conformational entropy change for the well-folded TAZ1 varies upon binding to different IDP targets. We further identify a cluster consisting of side chains in bound TAZ1 and CTAD-HIF-1α that experience extensive dynamics and are part of the binding region that involves the N-terminal end of the LPQL motif in CTAD-HIF-1α; a feature that might have an important role in the termination of the hypoxic response.

The magnitude of the backbone conformational entropy change in protein folding

1996 ◽  
Vol 25 (2) ◽  
pp. 143-156 ◽  
Author(s):  
J. Alejandro D'Aquino ◽  
Javier Gómez ◽  
Vincent J. Hilser ◽  
Kon Ho Lee ◽  
L. Mario Amzel ◽  
...  
Keyword(s):  
Protein Folding ◽  
Entropy Change ◽  
Conformational Entropy

Protein Folding: Solid evidence for molten globules

1994 ◽  
Vol 4 (7) ◽  
pp. 636-640 ◽  
Author(s):  
Christopher M. Dobson
Keyword(s):  
Protein Folding ◽  
Molten Globules

Empirical Scale of Side-Chain Conformational Entropy in Protein Folding

1993 ◽  
Vol 231 (3) ◽  
pp. 825-839 ◽  
Author(s):  
Stephen D. Pickett ◽  
Michael J.E. Sternberg
Keyword(s):  
Protein Folding ◽  
Side Chain ◽  
Conformational Entropy

scholarly journals Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations

2014 ◽  
Vol 111 (43) ◽  
pp. 15396-15401 ◽  
Author(s):  
M. C. Baxa ◽  
E. J. Haddadian ◽  
J. M. Jumper ◽  
K. F. Freed ◽  
T. R. Sosnick
Keyword(s):  
Protein Folding ◽  
Conformational Entropy

scholarly journals The Backbone Conformational Entropy of Protein Folding: Experimental Measures from Atomic Force Microscopy

2002 ◽  
Vol 322 (3) ◽  
pp. 645-652 ◽  
Author(s):  
James B. Thompson ◽  
Helen G. Hansma ◽  
Paul K. Hansma ◽  
Kevin W. Plaxco
Keyword(s):  
Atomic Force Microscopy ◽  
Protein Folding ◽  
Conformational Entropy ◽  
Force Microscopy ◽  
Atomic Force
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