Structural divergence is more extensive than sequence divergence for a family of intrinsically disordered proteins

Proteins: Structure, Function and Bioinformatics

Volumn 81, Issue 10, 2013, Pages 1686-1698

  Borcherds, Wade ^a   Kashtanov, Stepan ^a   Wu, Hongwei ^a   Daughdrill, Gary W ^a  

^a UNIVERSITY OF SOUTH FLORIDA   (United States)

Author keywords

Intrinsically disordered proteins; Protein dynamics; Structural divergence; Structural evolution

Indexed keywords

PROTEIN MDM2; PROTEIN P53; REPLICATION FACTOR A; SOLVENT; UBIQUITIN PROTEIN LIGASE E3;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; DYNAMICS; HUMAN; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; TRANSACTIVATION;

CANIS FAMILIARIS; CAVIA; MAMMALIA; ORYCTOLAGUS CUNICULUS;

INTRINSICALLY DISORDERED PROTEINS; PROTEIN DYNAMICS; STRUCTURAL DIVERGENCE; STRUCTURAL EVOLUTION;

AMINO ACID SEQUENCE; ANIMALS; CLUSTER ANALYSIS; DOGS; EVOLUTION, MOLECULAR; GUINEA PIGS; HUMANS; INTRINSICALLY DISORDERED PROTEINS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RABBITS; SEQUENCE ALIGNMENT; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84884207438     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24303     Document Type: Article

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