Amino acid substitutions affecting protein dynamics in eglin C do not affect heat capacity change upon unfolding

Proteins: Structure, Function and Genetics

Volumn 64, Issue 2, 2006, Pages 295-300

  Gribenko, Alexey V ^a   Keiffer, Timothy R ^a   Makhatadze, George I ^a  

^a PENN STATE COLLEGE OF MEDICINE   (United States)

Author keywords

Differential scanning calorimetry; Eglin C; Heat capacity change; Protein dynamics; Protein thermodynamics

Indexed keywords

EGLIN C; SERINE PROTEINASE INHIBITOR;

AMINO ACID SUBSTITUTION; ARTICLE; CALCULATION; CRYSTAL; DENSITY; DIFFERENTIAL SCANNING CALORIMETRY; HEAT TRANSFER; HYDRATION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; SURFACE PROPERTY; THERMODYNAMICS;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; BASE SEQUENCE; CALORIMETRY, DIFFERENTIAL SCANNING; HEAT; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEINS; TEMPERATURE; THERMODYNAMICS;

EID: 33745634372     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20974     Document Type: Article

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