Structural insights from 15N relaxation data for an anisotropic collagen peptide

Journal of the American Chemical Society

Volumn 131, Issue 51, 2009, Pages 18194-18195

  Xiao, Jianxi ^a   Baum, Jean ^a  

^a RUTGERS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE PROTON; CLEAVAGE SITES; COLLAGEN PEPTIDES; COLLAGEN-MODEL PEPTIDE; COLLAGENASE; DIFFUSION TENSOR; H-BONDING; H-BONDS; HELICAL PEPTIDE; HYDROGEN-BONDING EFFECTS; PROTEIN BACKBONE; RECOGNITION SITE; RELAXATION MEASUREMENTS; ROTATIONAL DIFFUSION; STRUCTURAL INFORMATION; STRUCTURAL INSIGHTS; STRUCTURE DETERMINATION;

AMIDES; ANISOTROPY; HYDROGEN; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES; PROTONS; TENSORS;

COLLAGEN;

COLLAGEN; NITROGEN 15;

ANISOTROPY; ARTICLE; CARBOXY TERMINAL SEQUENCE; DIFFUSION; DIFFUSION TENSOR IMAGING; HYDROGEN BOND; MUTATION; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PROTEIN ANALYSIS; PROTEIN STRUCTURE;

ANISOTROPY; COLLAGEN; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; NITROGEN ISOTOPES; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; ROTATION;

EID: 73249147315     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9056823     Document Type: Article

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20. RDCs could potentially provide a complementary approach for obtaining orientational information about the N-H bond vectors in triple-helical peptides. Attempts to find a suitable alignment medium (bicelles, gels, and pf1 phage) have to date been unsuccessful.