A "Link-Psi" strategy using crosslinking indicates that the folding transition state of ubiquitin is not very malleable

Protein Science

Volumn 21, Issue 6, 2012, Pages 819-827

  Shandiz, Ali T ^a   Baxa, Michael C ^a   Sosnick, Tobin R ^a  

^a UNIVERSITY OF CHICAGO   (United States)

Author keywords

Bihistidine; Crosslinking; Dichloroacetone; Heterogeneity; Metal binding; Psi analysis

Indexed keywords

ACETONE; GLOBULAR PROTEIN; HISTIDINE; METAL ION; UBIQUITIN;

ARTICLE; BINDING SITE; CONTROLLED STUDY; LIMIT OF DETECTION; MOLECULAR PROBE; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN FOLDING; PROTEIN POLYMORPHISM;

ACETONE; BINDING SITES; CROSS-LINKING REAGENTS; HALOGENATION; HISTIDINE; METALS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; UBIQUITIN;

EID: 84861443128     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2065     Document Type: Article

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