Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain

EMBO Journal

Volumn 16, Issue 20, 1997, Pages 6230-6236

  McCoy, Mark ^a,b   Stavridi, Elena S ^a   Waterman, Jennifer ^a   Wieczorek, Ania M ^a   Opella, Stanley J ^b   Halazonetls, Thanos D ^a,b  

^a WISTAR INSTITUTE   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Hydrophobic effect; Nmr spectroscopy; p53 tumor suppressor; Protein design; Protein structure

Indexed keywords

LEUCINE; PHENYLALANINE; PROTEIN P53;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; HUMAN; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN POLYMERIZATION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; STOICHIOMETRY;

AMINO ACID SEQUENCE; DIMERIZATION; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; TUMOR SUPPRESSOR PROTEIN P53;

EID: 0030722137     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.20.6230     Document Type: Article

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