Importance of the spatial display of charged residues in heparin-peptide interactions

Biopolymers

Volumn 93, Issue 3, 2010, Pages 290-298

  Rullo, Anthony ^a   Nitz, Mark ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

Circular dichroism; Fluorescence; Heparin; Peptides

Indexed keywords

AMINO ACID SEQUENCE; CHARGED RESIDUES; CIRCULAR DICHROISM; CONSENSUS SEQUENCE; GLYCOSAMINOGLYCANS; HEPARIN BINDING; HEPARIN BINDING PEPTIDES; HIGH AFFINITY; LINEAR DISTRIBUTION; POSITIVE CHARGES; SPATIAL ARRANGEMENTS; THREE ORDERS OF MAGNITUDE;

AMINO ACIDS; BINDING ENERGY; DICHROISM; FLUORESCENCE; ORGANIC ACIDS; PEPTIDES;

POLYSACCHARIDES;

HEPARIN; HEPARIN BINDING PROTEIN; PEPTIDE;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CIRCULAR DICHROISM; CONSENSUS SEQUENCE; PROTEIN BINDING; PROTEIN INTERACTION; ALPHA HELIX; CONTROLLED STUDY; DISSOCIATION CONSTANT; EQUILIBRIUM CONSTANT; PROTEIN CARBOHYDRATE INTERACTION; PROTEIN SECONDARY STRUCTURE; STRUCTURE ANALYSIS; SURFACE CHARGE;

AMINO ACID SEQUENCE; AMINO ACIDS; HEPARIN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN STRUCTURE, SECONDARY;

EID: 75149113108     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.21339     Document Type: Article

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