Dynamics of fd coat protein in lipid bilayers

Journal Article · Tue Feb 10 00:00:00 EST 1987 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00377a029· OSTI ID:6790814

Leo, G C; Colnago, L A; Valentine, K G; Opella, S J

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), Vol. 26:3
• Country of Publication: United States
• Language: English

Related Subjects

62 RADIOLOGY AND NUCLEAR MEDICINE
BACTERIOPHAGES
NUCLEAR MAGNETIC RESONANCE
LABELLED COMPOUNDS
NMR SPECTRA
PROTEINS
MOLECULAR STRUCTURE
AMINO ACIDS
DEUTERIUM COMPOUNDS
LIPIDS
MEMBRANES
PHOSPHOLIPIDS
PHOSPHORUS 31
CARBOXYLIC ACIDS
ESTERS
HYDROGEN COMPOUNDS
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
MICROORGANISMS
NUCLEI
ODD-EVEN NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC PHOSPHORUS COMPOUNDS
PARASITES
PHOSPHORUS ISOTOPES
RESONANCE
SPECTRA
STABLE ISOTOPES
VIRUSES
550601* - Medicine- Unsealed Radionuclides in Diagnostics