Thermodynamic analysis of α-spectrin SH3 and two of its circular permutants with different loop lengths: Discerning the reasons for rapid folding in proteins

Biochemistry

Volumn 38, Issue 2, 1999, Pages 549-559

  Martínez, Jose C ^a,b   Viguera, Ana R ^a   Berisio, Rita ^c   Wilmanns, Matthias ^c   Mateo, Pedro L ^b   Filimonov, Vladimir V ^b,d   Serrano, Luis ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b UNIVERSITY OF GRANADA   (Spain)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^d INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

FODRIN;

ARTICLE; CRYSTAL STRUCTURE; DIFFERENTIAL SCANNING CALORIMETRY; ENTHALPY; ENTROPY; FLOW KINETICS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FOLDING; SEQUENCE HOMOLOGY; THERMODYNAMICS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ASPARAGINE; ASPARTIC ACID; CALORIMETRY, DIFFERENTIAL SCANNING; COMPUTER SIMULATION; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN FOLDING; SPECTRIN; SRC HOMOLOGY DOMAINS; TEMPERATURE; THERMODYNAMICS;

EID: 0039726624     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi981515u     Document Type: Article

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