%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 }