Triple-helical peptides: An approach to collagen conformation, stability, and self-association

Biopolymers

Volumn 89, Issue 5, 2008, Pages 345-353

  Brodsky, Barbara ^a   Thiagarajan, Geetha ^a   Madhan, Balaraman ^a   Kar, Karunakar ^a  

^a RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

Author keywords

Collagen; Hydration; Hydrogen bonding; Peptides; Triple helix

Indexed keywords

AMINES; ASSOCIATION REACTIONS; HYDROGEN; HYDROGEN BONDS; MODEL STRUCTURES; NONMETALS; PEPTIDES; PROTEINS;

BIOPHYSICAL STUDIES; COLLAGEN TRIPLE-HELIX; HELICAL PARAMETERS; HELICAL PEPTIDES; HIGH-RESOLUTION STRUCTURES; HYDRATION; HYDROGEN BONDING; HYDROGEN BONDINGS; INTEGRAL PART; SELF ASSOCIATIONS; SEQUENCE-DEPENDENT; STRUCTURE-FUNCTION RELATIONSHIPS; TRIPLE HELIXES; TRIPLE-HELIX;

COLLAGEN;

COLLAGEN; COLLAGEN FIBER; COLLAGEN TYPE 1; COLLAGEN TYPE 3; COLLAGEN TYPE 4; GLYCINE; PEPTIDE DERIVATIVE; PEPTIDE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BIOPHYSICS; CALORIMETRY; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; COLLAGEN DISEASE; CRYSTAL STRUCTURE; DISEASE SEVERITY; EXTRACELLULAR MATRIX; HYDROGEN BOND; HYDROPHOBICITY; LIGAND BINDING; MATHEMATICAL COMPUTING; MISSENSE MUTATION; MOLECULAR MODEL; MUTATIONAL ANALYSIS; PHENOTYPE; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; SUPRAMOLECULAR CHEMISTRY; TISSUE REGENERATION; TRIPLE HELIX; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION; BIOLOGICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HUMAN; MUTATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; REVIEW;

COLLAGEN; CRYSTALLOGRAPHY, X-RAY; HUMANS; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MUTATION; PEPTIDES; PROTEIN CONFORMATION;

EID: 47749145413     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.20958     Document Type: Article

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