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Default Dynamics and Rigidity of an Intact Filamentous Bacteriophage Virus Probed by Magic Angle Spinning NMR.

Dynamics and Rigidity of an Intact Filamentous Bacteriophage Virus Probed by Magic Angle Spinning NMR.

Related Articles Dynamics and Rigidity of an Intact Filamentous Bacteriophage Virus Probed by Magic Angle Spinning NMR.

Chemistry. 2018 Apr 16;:

Authors: Aharoni T, Goldbourt A

Abstract
The capsid dynamics of filamentous bacteriophages is related to their function, stability and interactions with the genome, and can be assessed by measuring the chemical shift anisotropy (CSA) of 15N-amides, which are sensitive to large amplitude motions. In this study, we used CSA recoupling experiments under magic-angle spinning NMR in order to probe the dynamics of the y21m capsid mutant of fd bacteriophage. We show, based on fitting those generated CSA lineshapes, that residues located in the N-terminus undergo increased motional amplitudes suggesting its global motion, while other backbone residues are rigid, and imply on a tight hydrophobic packing of the phage.


PMID: 29660798 [PubMed - as supplied by publisher]



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