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

Tom Aharoni, Amir Goldbourt*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

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, CSA recoupling experiments under magic-angle spinning NMR were used to probe the dynamics of the y21m capsid mutant of fd bacteriophage. Based on fitting the generated CSA lineshapes, residues located in the N-terminus undergo increased motional amplitudes suggesting its global motion, whereas other backbone residues are rigid, and imply a tight hydrophobic packing of the phage.

Original languageEnglish
Pages (from-to)8737-8741
Number of pages5
JournalChemistry - A European Journal
Volume24
Issue number35
DOIs
StatePublished - 21 Jun 2018

Keywords

  • RNCSA
  • chemical shift anisotropy
  • fd filamentous bacteriophage
  • magic-angle spinning
  • protein dynamics
  • solid-State NMR

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