Conformational dynamics of an intact virus: order parameters for the coat protein of Pf1 bacteriophage.


This study has examined the atomic-level dynamics of the protein in the capsid of filamentous phage Pf1. This capsid consists of approximately 7,300 small subunits of only 46 aa in a helical array around a highly extended, circular single-stranded DNA molecule of 7,349 nt. Measurements were made of site-specific, solid-state NMR order parameters, S, the… (More)
DOI: 10.1073/pnas.0800405105


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