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Title: Nuclear magnetic resonance of the filamentous bacteriophage fd

Journal Article · · Biophys. J.; (United States)

The filamentous bacteriophage fd and its major coat protein are being studied by nuclear magnetic resonance (NMR) spectroscopy. /sup 31/P NMR shows that the chemical shielding tensor of the DNA phosphates of fd in solution is only slightly reduced in magnitude by motional averaging, indicating the DNA-protein interactions substantially immobilize the DNA packaged in the virus. There is no evidence of chemical interactions between the DNA backbone and the coat protein, since experiments on solid virus show the /sup 31/P resonances to have the same principal elements of its chemical shielding tensor as DNA. /sup 1/H and /sup 13/C NMR spectra of fd virus in solution indicate that the coat proteins are held rigidly in the structure except for some aliphatic side chains that undergo relatively rapid rotations. The presence of limited mobility in the viral coat proteins is substantiated by finding large quadrupole splittings in /sup 2/H NMR of deuterium labeled virions. The structure of the coat protein in a lipid environment differs significantly from that found for the assembled virus. Data from /sup 1/H and /sup 13/C NMR chemical shifts, amide proton exchange rates, and /sup 13/C relaxation measurements show that the coat protein in sodium dodecyl sulfate micelles has a native folded structure that varies from that of a typical globular protein or the coat protein in the virus by having a partially flexible backbone and some rapidly rotating aromatic rings.

Research Organization:
Univ. of Pennsylvania, Philadelphia, PA (United States)
OSTI ID:
7032424
Journal Information:
Biophys. J.; (United States), Vol. 32:1
Country of Publication:
United States
Language:
English