Unfolding Simulations Reveal the Mechanism of Extreme Unfolding Cooperativity in the Kinetically Stable α-Lytic Protease-Reference-Cited by-同舟云学术

Unfolding Simulations Reveal the Mechanism of Extreme Unfolding Cooperativity in the Kinetically Stable α-Lytic Protease

Published:2010-02-26 Issue:2 Volume:6 Page:e1000689
ISSN:1553-7358
Container-title:PLoS Computational Biology
language:en
Short-container-title:PLoS Comput Biol

Author:

Salimi Neema L.,Ho Bosco,Agard David A.

Publisher

Public Library of Science (PLoS)

Subject

Computational Theory and Mathematics,Cellular and Molecular Neuroscience,Genetics,Molecular Biology,Ecology,Modeling and Simulation,Ecology, Evolution, Behavior and Systematics

Reference59 articles.

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4. Disabling the folding catalyst is the last critical step in alpha-lytic protease folding.;EL Cunningham;Protein Sci,2004

5. Comprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases.;SS Jaswal;J Mol Biol,2005

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