%0 Journal Article %1 thiriot_structural_2005 %A Thiriot, David S %A Nevzorov, Alexander A %A Opella, Stanley J %D 2005 %J Protein Sci. %K Acid Amino Data,Nuclear Magnetic Proteins,Molecular Resonance,Temperature Sequence Sequence,Biomolecular,Capsid %N 4 %P 1064--1070 %R 10.1110/ps.041220305 %T Structural basis of the temperature transition of \Pf\1 bacteriophage %V 14 %X 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 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.

@article{thiriot_structural_2005, abstract = {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 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.}, added-at = {2017-03-14T02:48:56.000+0100}, author = {Thiriot, David S and Nevzorov, Alexander A and Opella, Stanley J}, biburl = {https://www.bibsonomy.org/bibtex/2842e3adc3c1f39f6022b455be9375cfb/nmrresource}, doi = {10.1110/ps.041220305}, interhash = {502e60a4ac7fa788a0295caea8f73933}, intrahash = {842e3adc3c1f39f6022b455be9375cfb}, issn = {0961-8368}, journal = {Protein Sci.}, keywords = {Acid Amino Data,Nuclear Magnetic Proteins,Molecular Resonance,Temperature Sequence Sequence,Biomolecular,Capsid}, month = apr, number = 4, pages = {1064--1070}, pmid = {15741342}, timestamp = {2017-03-14T02:49:21.000+0100}, title = {{Structural basis of the temperature transition of {\{}Pf{\}}1 bacteriophage}}, volume = 14, year = 2005 }