Heparin binding to platelet factor-4. An NMR and site-directed mutagenesis study: arginine residues are crucial for binding.
Mayo, K H
Heparin binding to platelet factor-4. An NMR and site-directed mutagenesis study: arginine residues are crucial for binding. [electronic resource] - The Biochemical journal Dec 1995 - 357-65 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
0264-6021
10.1042/bj3120357 doi
Amino Acid Sequence
Arginine
Binding Sites
Genes, Synthetic
Heparin--metabolism
Humans
Kinetics
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Platelet Factor 4--biosynthesis
Protein Folding
Protein Structure, Secondary
Recombinant Proteins--biosynthesis
Heparin binding to platelet factor-4. An NMR and site-directed mutagenesis study: arginine residues are crucial for binding. [electronic resource] - The Biochemical journal Dec 1995 - 357-65 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
0264-6021
10.1042/bj3120357 doi
Amino Acid Sequence
Arginine
Binding Sites
Genes, Synthetic
Heparin--metabolism
Humans
Kinetics
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Platelet Factor 4--biosynthesis
Protein Folding
Protein Structure, Secondary
Recombinant Proteins--biosynthesis