Hydrogen exchange of the tetramerization domain of the human tumour suppressor p53 probed by denaturants and temperature

European Journal of Biochemistry

Volumn 268, Issue 18, 2001, Pages 4868-4877

  Neira, José L ^a,b   Mateu, Mauricio G ^a,b  

^a MIGUEL HERNÁNDEZ UNIVERSITY   (Spain)

^b UNIVERSIDAD AUTÓNOMA DE MADRID   (Spain)

Author keywords

Denaturation; Hydrogen exchange; Protein folding; Stability

Indexed keywords

AMIDE; CHLORIDE; DEUTERIUM; GUANIDINE; HYDROGEN; MONOMER; PROTEIN P53; PROTON; TETRAMER;

ALPHA HELIX; ARTICLE; BETA SHEET; CHEMICAL ANALYSIS; CIRCULAR DICHROISM; ENTHALPY; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; TEMPERATURE; THERMODYNAMICS;

DIMERIZATION; GUANIDINE; HUMANS; HYDROGEN; HYDROGEN BONDING; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; TEMPERATURE; THERMODYNAMICS; TUMOR SUPPRESSOR PROTEIN P53;

EID: 0034786608     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2001.02414.x     Document Type: Article

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