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Dynamics and Rigidity of an Intact Filamentous Bacteriophage Virus Probed by Magic Angle Spinning NMR
Author(s) -
Aharoni Tom,
Goldbourt Amir
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201800532
Subject(s) - capsid , magic angle spinning , bacteriophage , filamentous bacteriophage , chemistry , biophysics , mutant , molecular dynamics , dynamics (music) , chemical physics , crystallography , nuclear magnetic resonance spectroscopy , physics , stereochemistry , biology , computational chemistry , biochemistry , escherichia coli , gene , acoustics
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 15 N 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.