Influence of the hydrophilic face on the folding ability and stability of α-helix bundles: Relevance to the peptide catalytic activity

Journal of Peptide Research

Volumn 56, Issue 3, 2000, Pages 121-131

  Blondelle, S E ^a   Esteve, V ^b   Celda, B ^b   Pastor, M T ^a,b   Perez Paya E ^a,b  

^a TORREY PINES INSTITUTE FOR MOLECULAR STUDIES   (United States)

^b UNIVERSITY OF VALENCIA   (Spain)

Author keywords

helical bundle; Catalytic activity; Folding stability; Peptide self assembly; Protein design

Indexed keywords

OXALOACETIC ACID; SYNTHETIC PEPTIDE;

ALPHA HELIX; ANISOTROPY; ARTICLE; CATALYST; CIRCULAR DICHROISM; DECARBOXYLATION; FLUORESCENCE; HYDROPHILICITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; THERMOSTABILITY;

AMINO ACID SEQUENCE; AMINO ACIDS; ANILINO NAPHTHALENESULFONATES; ANISOTROPY; CATALYTIC DOMAIN; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; DECARBOXYLATION; ENZYME STABILITY; FLUORESCENCE; GUANIDINE; HEAT; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXALOACETATE; PEPTIDE FRAGMENTS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

EID: 0033823613     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.2000.00744.x     Document Type: Article

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