Filling a cavity dramatically increases pressure stability of the c-Myb R2 subdomain

Proteins: Structure, Function and Genetics

Volumn 45, Issue 1, 2001, Pages 96-101

  Eriksen, Tine A ^a,b   Wright, David M ^a,b   Purslow, Peter P ^b   Duance, Victor C ^a  

^a CARDIFF UNIVERSITY   (United Kingdom)

^b UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

C Myb; Cavity volume; High pressure NMR; Mutation; Partial molar volume; Thermodynamic stability; Volume change upon unfolding

Indexed keywords

GLOBULAR PROTEIN; PROTEIN C MYB;

ARTICLE; MUTATION; PRESSURE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTON NUCLEAR MAGNETIC RESONANCE; THERMODYNAMICS; THERMOSTABILITY;

MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MUTATION; PRESSURE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RENATURATION; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-MYB; THERMODYNAMICS;

EID: 0035479686     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.1128     Document Type: Article

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