Is there an en route folding intermediate for cold shock proteins?
Author:
Funder
NIH
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2053/fullpdf
Reference66 articles.
1. Universal nucleic acid-binding domain revealed by crystal-structure of the bacillus-subtilis major cold-shock protein;Schindelin;Nature,1993
2. Structure and function of bacterial cold shock proteins;Horn;Cell Mol Life Sci,2007
3. Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins;Perl;Nat Struct Biol,1998
4. Extremely rapid protein-folding in the absence of intermediates;Schindler;Nat Struct Biol,1995
5. Thermodynamic properties of an extremely rapid protein folding reaction;Schindler;Biochemistry,1996
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1. Intrinsic Disorder in a Well-Folded Globular Protein;The Journal of Physical Chemistry B;2018-02-01
2. The Small β-barrel Domain: A Survey-based Structural Analysis;2017-05-22
3. Cold Shock Protein A from Corynebacterium pseudotuberculosis: Role of Electrostatic Forces in the Stability of the Secondary Structure;Protein & Peptide Letters;2017-03-08
4. Toward a quantitative description of microscopic pathway heterogeneity in protein folding;Physical Chemistry Chemical Physics;2017
5. A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution;Nature Communications;2016-06-01
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