The pH dependence of hydrogen-deuterium exchange in trp repressor: The exchange rate of amide protons in proteins reflects tertiary interactions, not only secondary structure

Protein Science

Volumn 5, Issue 4, 1996, Pages 653-662

  Finucane, Michael D ^a,b   Jardetzky, Oleg ^a  

^a STANFORD UNIVERSITY   (United States)

^b UNIVERSITY OF SUSSEX   (United Kingdom)

Author keywords

acid denaturation; amide proton hydrogen exchange; local unfolding; nuclear magnetic resonance; proteins

Indexed keywords

DEUTERIUM; HYDROGEN; REPRESSOR PROTEIN;

ANION EXCHANGE; ARTICLE; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN STABILITY; REPRESSOR GENE; STRUCTURE ANALYSIS;

EID: 0029875082     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050409     Document Type: Article

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