Article,

Effects of temperature and \Y\21M mutation on conformational heterogeneity of the major coat protein (\pVIII\) of filamentous bacteriophage fd

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J. Mol. Biol., 286 (3): 787--796 (February 1999)
DOI: 10.1006/jmbi.1998.2517

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.

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