Molecular dynamics simulations of the native and partially folded states of ubiquitin: Influence of methanol cosolvent, pH, and temperature on the protein structure and dynamics-Reference-Cited by-同舟云学术

Molecular dynamics simulations of the native and partially folded states of ubiquitin: Influence of methanol cosolvent, pH, and temperature on the protein structure and dynamics

Published:2007-06 Issue:6 Volume:16 Page:1101-1118
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Sci.

Author:

Kony David B.,Hünenberger Philippe H.,van Gunsteren Wilfred F.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference67 articles.

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2. Molecular dynamics simulations of protein unfolding and limited refolding: Characterization of partially unfolded states of ubiquitin in 60% methanol and in water;Alonso;J. Mol. Biol.,1995

3. Role of the molten globule state in protein folding;Arai;Adv. Protein Chem.,2000

4. Monte-Carlo studies of the dielectric properties of water-like models;Barker;Mol. Phys.,1973

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