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.
%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
}