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Biochemistry / Phi value analysis / Protein domain / Protein folding / Serpin / Thermostability / Protease / Enzyme / Protein structure / Biology / Chemistry


J. Mol. Biol[removed], 784–795 doi:[removed]j.jmb[removed]Mesophile versus Thermophile: Insights Into the Structural Mechanisms of Kinetic Stability
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Document Date: 2007-06-14 17:08:33

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City

La Jolla / San Francisco / Green / Montreal / Dima / /

Company

Pymol.58 Protein Data Bank / Hercules / Elsevier Ltd. / RCSB Protein Data Bank / C2 / Millipore / Sigma Aldrich / /

Country

Canada / /

Currency

pence / /

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Facility

Cornell University / bridge of TFPA / bridge of αLP / Howard Hughes Medical Institute / Agard laboratory / University of California / /

IndustryTerm

active site / free energy unfolding barrier / large free energy barriers / search model / cleavage site / free energy / online version / large free energy barrier / free energy barrier / large unfolding free energy barrier / chemicals / Steel springs / space / larger unfolding free energy barrier / energy / /

Organization

Department of Biochemistry and Biophysics / University of California / San Francisco / Howard Hughes Medical Institute / Cornell University / /

Person

David Wilson / G. Murshudov / David A. Agard / Diane Irwin / Brian A. Kelch / /

Position

Butler / corresponding author / /

Product

acetic acid / sodium acetate / potassium acetate / /

ProvinceOrState

Rhode Island / Nova Scotia / California / /

Technology

alpha / thermodynamics / X-ray / Directed Mutagenesis / Crystallization / DNA binding / /

URL

http /

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