Dynamics of fd coat protein in lipid bilayers.
The dynamics of backbone and side-chain sites of the membrane-bound form of fd coat protein are described with solid-state 2H and 15N NMR experiments. The samples were isotopically labeled coat protein in phospholipid bilayers in excess water. The protein itself is immobile and does not undergo rapid rotation within the bilayer. Like the structural form of the protein, the membrane-bound form has four mobile residues at the N-terminus. The membrane-bound form differs from the structural form in having several mobile residues at the C-terminus. Many of the side chains of residues with immobile backbone sites undergo large amplitude jump motions. The dynamics are generally similar in both the structural and membrane-bound forms of the protein.
D015060:1,2-Dipalmitoylphosphatidylcholine; D002213:Capsid; D002918:Chymotrypsin; D003090:Coliphages; D004134:Dimyristoylphosphatidylcholine; D004926:Escherichia coli; D008051:Lipid Bilayers; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation
D008051:Lipid Bilayers; D010446:Peptide Fragments; D015060:1,2-Dipalmitoylphosphatidylcholine; D002918:Chymotrypsin; D004134:Dimyristoylphosphatidylcholine