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.
Original language | English |
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Pages (from-to) | 787-796 |
Number of pages | 10 |
Journal | Journal of Molecular Biology |
Volume | 286 |
Issue number | 3 |
DOIs | |
State | Published - 26 Feb 1999 |
Externally published | Yes |
Keywords
- Filamentous bacteriophage
- Major coat protein
- Solid-state NMR spectroscopy
- fd
- pVIII
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology