Thermodynamic and structural consequences of flexible loop deletion by circular permutation in the streptavidin-biotin system

Protein Science

Volumn 7, Issue 4, 1998, Pages 848-859

  Chu, Vano ^a   Freitag, Stefanie ^a,b   Trong, Isolde L E ^b   Stenkamp, Ronald E ^b   Stayton, Patrick S ^a  

^a University of Washington   (United States)

^b UNIVERSITY OF WASHINGTON   (United States)

Author keywords

Circular permutation; Ligand binding thermodynamics; Loop deletion; Molecular recognition; Streptavidin; Structure based drug design

Indexed keywords

BIOTIN; STREPTAVIDIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CALORIMETRY; CARBOXY TERMINAL SEQUENCE; CHEMICAL STRUCTURE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENTHALPY; ENTROPY; HYDROGEN BOND; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; THERMODYNAMICS;

EID: 0031956609     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070403     Document Type: Article

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