Structural basis for the difference in thermodynamic properties between the two cysteine proteinase inhibitors human stefins a and b

Protein Engineering, Design and Selection

Volumn 7, Issue 8, 1994, Pages 977-984

  Jerala, Roman ^a   žerovnik, Eva ^a   Lohner, Karl ^a,b   Turk, Vito ^a  

^a JO EF STEFAN INSTITUTE   (Slovenia)

^b ERICH SCHMID INSTITUTE OF MATERIALS SCIENCE   (Austria)

Author keywords

Cysteine proteinase inhibitor; Homology modelling; Molten globule; Structural thermodynamics; Thermostability

Indexed keywords

CYSTEINE PROTEINASE INHIBITOR; GLOBULAR PROTEIN; STEFIN A; STEFIN B;

ARTICLE; CALORIMETRY; HYDRATION; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; THERMODYNAMICS; THERMOSTABILITY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BASE SEQUENCE; CALORIMETRY; COMPARATIVE STUDY; COMPUTER SIMULATION; CYSTATINS; ESCHERICHIA COLI; EVALUATION STUDIES; HEAT; HUMAN; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUPPORT, NON-U.S. GOV'T; THERMODYNAMICS;

EID: 0028030936     PISSN: 17410126     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/7.8.977     Document Type: Article

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