Effects of temperature and Y21M mutation on conformational heterogeneity of the major coat protein (pVIII) of filamentous bacteriophage fd.
J Mol Biol
; 286(3): 787-96, 1999 Feb 26.
Article
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| MEDLINE
| ID: mdl-10024451
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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Base de datos:
MEDLINE
Asunto principal:
Conformación Proteica
/
Proteínas Virales
/
Inovirus
/
Mutación
Idioma:
En
Revista:
J Mol Biol
Año:
1999
Tipo del documento:
Article