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Comparison of the dynamics of the membrane‐bound form of fd coat protein in micelles and in bilayers by solution and solid‐state nitrogen‐15 nuclear magnetic resonance spectroscopy
Author(s) -
Bogusky M. J.,
Leo G. C.,
Opella S. J.
Publication year - 1988
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340040205
Subject(s) - micelle , chemistry , membrane , crystallography , solid state nuclear magnetic resonance , phospholipid , nuclear magnetic resonance spectroscopy , biophysics , analytical chemistry (journal) , nuclear magnetic resonance , stereochemistry , biochemistry , chromatography , organic chemistry , aqueous solution , biology , physics
Solid‐state and solution 15 N nuclear magnetic resonance experiments on uniformly and specifically 15 N labeled coat protein in phospholipid bilayers and in detergent micelles are used to describe the dynamics of the membrane‐bound form of the protein. The residues in the N‐ and C‐terminal portions of the coat protein in both phospholipid bilayers and in detergent micelles are mobile, while those in the hydrophobic midsection are immobile. There is evidence for a gradient of mobility in the C‐terminal region of the coat protein in micelles; at 25°C only the last two residues are mobile on the 10 9 ‐Hz timescale, while the last six to eight residues appear to be mobile on slower timescales and highly mobile at higher temperatures. Since all of the C‐terminal residues are immobile in the virus particles, the mobility of these residues in the membrane‐bound form of the protein may be important for the formation of protein‐DNA interactions in the assembly process.