Journal
PROTEIN SCIENCE
Volume 14, Issue 4, Pages 1064-1070Publisher
WILEY
DOI: 10.1110/ps.041220305
Keywords
NMR; filamentous bacteriophage; temperature transition; protein structure
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Funding
- NIBIB NIH HHS [R01 EB 002169, P41 EB002031, R01 EB002169, P41 EB 002031, R01 EB 001966, R01 EB001966] Funding Source: Medline
- NIGMS NIH HHS [F32 GM063300, F32 GM 63300] Funding Source: Medline
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The filamentous bacteriophage Pfl undergoes a reversible temperature-dependent transition that is also influenced by salt concentrations. This structural responsiveness may be a manifestation of the important biological property of flexibility, which is necessary for long, thin filamentous assemblies as a protection against shear forces. To investigate structural changes in the major coat protein, one- and two-dimensional solid-state NMR spectra of concentrated solutions of Pfl bacteriophage were acquired, and the structure of the coat protein determined at 0 degrees C was compared with the structure previously determined at 30 degrees C. Despite dramatic differences in the NMR spectra, the overall change in the coat protein structure is small. Changes in the orientation of the C-terminal helical segment and the conformation of the first five residues at the N-terminus are apparent. These results are consistent with prior studies by X-ray fiber diffraction and other biophysical methods.
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