%0 Journal Article %1 schiksnis_structure_1987 %A Schiksnis, R A %A Bogusky, M J %A Tsang, P %A Opella, S J %D 1987 %J Biochemistry %K Amides,Capsid,Coliphages,Hydrogen Analysis,Tyrosine Bonding,Magnetic Conformation,Spectrum Proteins,Micelles,Protein Resonance Spectroscopy,Membrane %N 5 %P 1373--1381 %T Structure and dynamics of the \Pf\1 filamentous bacteriophage coat protein in micelles %V 26 %X The major coat protein of filamentous bacteriophage adopts its membrane-bound conformation in detergent micelles. High-resolution 1H and 15N NMR experiments are used to characterize the structure and dynamics of residues 30-40 in the hydrophobic midsection of Pf1 coat protein in sodium dodecyl sulfate micelles. Uniform and specific-site 15N labels enable the immobile backbone sites to be identified by their 1H/15N heteronuclear nuclear Overhauser effect and allow the assignment of 1H and 15N resonances. About one-third of the amide N-H protons in the protein undergo very slow exchange with solvent deuterons, which is indicative of sites in highly structured environments. The combination of results from 1H/15N heteronuclear correlation, 1H homonuclear correlation, and 1H homonuclear Overhauser effect experiments assigns the resonances to specific residues and demonstrates that residues 30-40 of the coat protein have a helical secondary structure.

@article{schiksnis_structure_1987, abstract = {The major coat protein of filamentous bacteriophage adopts its membrane-bound conformation in detergent micelles. High-resolution 1H and 15N NMR experiments are used to characterize the structure and dynamics of residues 30-40 in the hydrophobic midsection of Pf1 coat protein in sodium dodecyl sulfate micelles. Uniform and specific-site 15N labels enable the immobile backbone sites to be identified by their 1H/15N heteronuclear nuclear Overhauser effect and allow the assignment of 1H and 15N resonances. About one-third of the amide N-H protons in the protein undergo very slow exchange with solvent deuterons, which is indicative of sites in highly structured environments. The combination of results from 1H/15N heteronuclear correlation, 1H homonuclear correlation, and 1H homonuclear Overhauser effect experiments assigns the resonances to specific residues and demonstrates that residues 30-40 of the coat protein have a helical secondary structure.}, added-at = {2017-03-14T02:48:56.000+0100}, author = {Schiksnis, R A and Bogusky, M J and Tsang, P and Opella, S J}, biburl = {https://www.bibsonomy.org/bibtex/2ec9c729b54f771309202662714fb4b16/nmrresource}, interhash = {ba6667dc07cee0552ebe967f562ce954}, intrahash = {ec9c729b54f771309202662714fb4b16}, issn = {0006-2960}, journal = {Biochemistry}, keywords = {Amides,Capsid,Coliphages,Hydrogen Analysis,Tyrosine Bonding,Magnetic Conformation,Spectrum Proteins,Micelles,Protein Resonance Spectroscopy,Membrane}, month = mar, number = 5, pages = {1373--1381}, pmid = {3567175}, timestamp = {2017-03-14T02:49:21.000+0100}, title = {{Structure and dynamics of the {\{}Pf{\}}1 filamentous bacteriophage coat protein in micelles}}, volume = 26, year = 1987 }