%0 Journal Article %1 bogusky_comparison_1988 %A Bogusky, M J %A Leo, G C %A Opella, S J %D 1988 %J Proteins %K 1,2-Dipalmitoylphosphatidylcholine,Colloids,DNA-Binding Conformation,Viral Isotopes,Protein Proteins Proteins,Dimyristoylphosphatidylcholine,Lipid Resonance Spectroscopy,Micelles,Nitrogen bilayers,Magnetic %N 2 %P 123--130 %R 10.1002/prot.340040205 %T 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 %V 4 %X Solid-state and solution 15N nuclear magnetic resonance experiments on uniformly and specifically 15N 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 degrees 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.

@article{bogusky_comparison_1988, abstract = {Solid-state and solution 15N nuclear magnetic resonance experiments on uniformly and specifically 15N 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 degrees 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.}, added-at = {2017-03-14T02:48:56.000+0100}, author = {Bogusky, M J and Leo, G C and Opella, S J}, biburl = {https://www.bibsonomy.org/bibtex/2cecba9edc85d0592ff152e7e0fe00b04/nmrresource}, doi = {10.1002/prot.340040205}, interhash = {ea949663ef75f4029ff1e83ff44101b5}, intrahash = {cecba9edc85d0592ff152e7e0fe00b04}, issn = {0887-3585}, journal = {Proteins}, keywords = {1,2-Dipalmitoylphosphatidylcholine,Colloids,DNA-Binding Conformation,Viral Isotopes,Protein Proteins Proteins,Dimyristoylphosphatidylcholine,Lipid Resonance Spectroscopy,Micelles,Nitrogen bilayers,Magnetic}, number = 2, pages = {123--130}, pmid = {3227013}, timestamp = {2017-03-14T02:49:21.000+0100}, title = {{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}}, volume = 4, year = 1988 }