Dynamics of fd coat protein in lipid bilayers
The dynamics of backbone and side-chains sites of the membrane-bound form of fd coat protein are described with solid-state /sup 2/H and /sup 15/N 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.
- Research Organization:
- Univ. of Pennsylvania, Philadelphia
- OSTI ID:
- 6790814
- Journal Information:
- Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 26:3; ISSN BICHA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
62 RADIOLOGY AND NUCLEAR MEDICINE
AMINO ACIDS
BACTERIOPHAGES
CARBOXYLIC ACIDS
DEUTERIUM COMPOUNDS
ESTERS
HYDROGEN COMPOUNDS
ISOTOPES
LABELLED COMPOUNDS
LIGHT NUCLEI
LIPIDS
MAGNETIC RESONANCE
MEMBRANES
MICROORGANISMS
MOLECULAR STRUCTURE
NMR SPECTRA
NUCLEAR MAGNETIC RESONANCE
NUCLEI
ODD-EVEN NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC PHOSPHORUS COMPOUNDS
PARASITES
PHOSPHOLIPIDS
PHOSPHORUS 31
PHOSPHORUS ISOTOPES
PROTEINS
RESONANCE
SPECTRA
STABLE ISOTOPES
VIRUSES