Solvent-exposed residues located in the β-sheet modulate the stability of the tetramerization domain of p53-A structural and combinatorial approach

Proteins: Structure, Function and Genetics

Volumn 71, Issue 4, 2008, Pages 1670-1685

  Mora, Puig ^a   Carbajo, Rodrigo J ^a   Pineda Lucena, Antonio ^a   Sánchez Del Pino, Manuel M ^a   Pérez Payá, Enrique ^b  

^a CENTRO DE INVESTIGACIÓN PRÍNCIPE FELIPE   (Spain)

^b INSTITUTO DE BIOMEDICINA DE VALENCIA   (Spain)

Author keywords

Combinatorial library; Hydrophobicity; NMR; Protein stability; Secondary structure propensity; Solvent exposed residues; Tetramerization domain of p53

Indexed keywords

GLYCINE; MUTANT PROTEIN; PROTEIN P53; SOLVENT; TETRAMER; THREONINE; TYROSINE;

ARTICLE; BETA SHEET; BIOPHYSICS; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; RESIDUE ANALYSIS; TEMPERATURE; THERMODYNAMICS; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACIDS; BIOPHYSICS; CIRCULAR DICHROISM; COMBINATORIAL CHEMISTRY TECHNIQUES; DIMERIZATION; GLYCINE; GUANIDINE; HEAT; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE LIBRARY; PEPTIDES; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SOLVENTS; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE; THERMODYNAMICS; THREONINE; TUMOR SUPPRESSOR PROTEIN P53; TYROSINE;

EID: 44349183748     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21854     Document Type: Article

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