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Structural basis of the temperature transition of Pf1 bacteriophage

Department of Chemistry and Biochemistry, University of California–San Diego, La Jolla, California 92093-0307, USA

(RECEIVED November 8, 2004; FINAL REVISION December 21, 2004; ACCEPTED December 21, 2004)

The filamentous bacteriophage Pf1 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 Pf1 bacteriophage were acquired, and the structure of the coat protein determined at 0°C was compared with the structure previously determined at 30°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.

Keywords: NMR; filamentous bacteriophage; temperature transition; protein structure

Abbreviations: NMR, nuclear magnetic resonance • DNA, deoxyribonucleic acid • RMSD, root-mean-square deviation

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.041220305.

Reprint requests to: Stanley J. Opella, Department of Chemistry and Biochemistry, University of California–San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0307, USA; e-mail: sopella{at}ucsd.edu; fax: (858) 822-4821.

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