Intersubunit Hydrophobic Interactions in Pf1 Filamentous Phage |
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Authors: | Amir Goldbourt Loren A. Day Ann E. McDermott |
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Affiliation: | From the ‡School of Chemistry, Tel Aviv University, Ramat Aviv 69978, Tel Aviv, Israel.;the §Public Health Research Institute, University of Medicine and Dentistry of New Jersey, Newark, New Jersey 07103, and ;the ¶Department of Chemistry, Columbia University, New York, New York 10027 |
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Abstract: | Magic angle spinning solid-state NMR has been used to study the structural changes in the Pf1 filamentous bacteriophage, which occur near 10 °C. Comparisons of NMR spectra recorded above and below 10 °C reveal reversible perturbations in many NMR chemical shifts, most of which are assigned to atoms of hydrophobic side chains of the 46-residue subunit. The changes mainly involve groups located in patches on the interfaces between neighboring capsid subunits. The observations show that the transition adjusts the hydrophobic interfaces between fairly rigid subunits. The low temperature form has been generally more amenable to structure determination; spin diffusion experiments on this form revealed unambiguous contacts between side chains of neighboring subunits. These contacts are important constraints for structure modeling. |
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Keywords: | Bacteriophage NMR Protein Assembly Protein Structure Spectroscopy Hydrophobic Interactions Magic Angle Spinning Phase Transition |
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