Factors governing 310-helix vs α-helix formation in peptides: Percentage of cα-tetrasubstituted α-amino acid residues and sequence dependence

Biopolymers

Volumn 64, Issue 5, 2002, Pages 236-245

  Crisma, Marco ^a   Bisson, William ^a   Formaggio, Fernando ^a   Broxterman, Quirinus B ^b   Toniolo, Claudio ^a  

^a UNIVERSITY OF PADOVA   (Italy)

^b DSM Fine Chemicals Austria Nfg GmbH & Co KG   (Netherlands)

Author keywords

C tetrasubstitution in amino acids; Type of helical structure; Type of peptide helix; X ray diffraction analysis of oligopeptides; X ray diffraction of peptides

Indexed keywords

AMINO ACIDS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PLASTICITY; X RAY DIFFRACTION;

HELICAL CONFORMATION;

BIOPOLYMERS;

ALPHA AMINO ACID; PEPTIDE;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; PEPTIDE ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; AMINO ACIDS; BIOPOLYMERS; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; MODELS, MOLECULAR; OLIGOPEPTIDES; PROTEIN STRUCTURE, SECONDARY;

IVA;

EID: 0037102908     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/bip.10178     Document Type: Article

References (62)