Both helical propensity and side-chain hydrophobicity at a partially exposed site in α-helix contribute to the thermodynamic stability of ubiquitin

Proteins: Structure, Function and Genetics

Volumn 58, Issue 1, 2005, Pages 1-6

  Loladze, Vakhtang V ^a   Makhatadze, George I ^a  

^a PENN STATE COLLEGE OF MEDICINE   (United States)

Author keywords

Differential scanning calorimetry; Helical propensity; Hydrophobicity; Protein engineering; Protein stability

Indexed keywords

UBIQUITIN;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; CORRELATION ANALYSIS; DIFFERENTIAL SCANNING CALORIMETRY; ENTHALPY; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ENGINEERING; PROTEIN EXPRESSION; PROTEIN STABILITY; RESIDUE ANALYSIS; THERMODYNAMICS; THERMOSTABILITY;

ESCHERICHIA COLI PROTEINS; HYDROPHOBICITY; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS; UBIQUITIN; VARIATION (GENETICS);

EID: 10844292653     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20283     Document Type: Article

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