Solid-state NMR spectroscopy was used to analyze the conformational heterogeneity of the major coat protein (pVIII) of filamentous bacteriophage fd. Both one and two-dimensional solid-state NMR spectra of magnetically aligned samples of fd bacteriophage reveal that an increase in temperature and a single site substitution (Tyr21 to Met, Y21M) reduce the conformational heterogeneity observed throughout wild-type pVIII. The NMR results are consistent with previous studies indicating that conformational flexibility in the hinge-bend segment that links the amphipathic and hydrophobic helices in the membrane-bound form of the protein plays an essential role during phage assembly, which involves a major change in the tertiary, but not secondary, structure of the coat protein.
%0 Journal Article
%1 tan_effects_1999
%A Tan, W M
%A Jelinek, R
%A Opella, S J
%A Malik, P
%A Terry, T D
%A Perham, R N
%D 1999
%J J. Mol. Biol.
%K Capsid,Inovirus,Magnetic Conformation,Protein Isotopes,Protein Proteins Resonance Spectroscopy,Mutagenesis,Mutation,Nitrogen Structure,Secondary,Site-Directed,Temperature,Tertiary,Viral
%N 3
%P 787--796
%R 10.1006/jmbi.1998.2517
%T Effects of temperature and \Y\21M mutation on conformational heterogeneity of the major coat protein (\pVIII\) of filamentous bacteriophage fd
%V 286
%X Solid-state NMR spectroscopy was used to analyze the conformational heterogeneity of the major coat protein (pVIII) of filamentous bacteriophage fd. Both one and two-dimensional solid-state NMR spectra of magnetically aligned samples of fd bacteriophage reveal that an increase in temperature and a single site substitution (Tyr21 to Met, Y21M) reduce the conformational heterogeneity observed throughout wild-type pVIII. The NMR results are consistent with previous studies indicating that conformational flexibility in the hinge-bend segment that links the amphipathic and hydrophobic helices in the membrane-bound form of the protein plays an essential role during phage assembly, which involves a major change in the tertiary, but not secondary, structure of the coat protein.
@article{tan_effects_1999,
abstract = {Solid-state NMR spectroscopy was used to analyze the conformational heterogeneity of the major coat protein (pVIII) of filamentous bacteriophage fd. Both one and two-dimensional solid-state NMR spectra of magnetically aligned samples of fd bacteriophage reveal that an increase in temperature and a single site substitution (Tyr21 to Met, Y21M) reduce the conformational heterogeneity observed throughout wild-type pVIII. The NMR results are consistent with previous studies indicating that conformational flexibility in the hinge-bend segment that links the amphipathic and hydrophobic helices in the membrane-bound form of the protein plays an essential role during phage assembly, which involves a major change in the tertiary, but not secondary, structure of the coat protein.},
added-at = {2017-03-14T02:48:56.000+0100},
author = {Tan, W M and Jelinek, R and Opella, S J and Malik, P and Terry, T D and Perham, R N},
biburl = {https://www.bibsonomy.org/bibtex/27d25315ea9c1bdb0bfb3a483844bbc13/nmrresource},
doi = {10.1006/jmbi.1998.2517},
interhash = {4a3134049817167c920b4941957148ba},
intrahash = {7d25315ea9c1bdb0bfb3a483844bbc13},
issn = {0022-2836},
journal = {J. Mol. Biol.},
keywords = {Capsid,Inovirus,Magnetic Conformation,Protein Isotopes,Protein Proteins Resonance Spectroscopy,Mutagenesis,Mutation,Nitrogen Structure,Secondary,Site-Directed,Temperature,Tertiary,Viral},
month = feb,
number = 3,
pages = {787--796},
pmid = {10024451},
timestamp = {2017-03-14T02:49:21.000+0100},
title = {{Effects of temperature and {\{}Y{\}}21M mutation on conformational heterogeneity of the major coat protein ({\{}pVIII{\}}) of filamentous bacteriophage fd}},
volume = 286,
year = 1999
}