title: Magic-angle spinning NMR of a class I filamentous bacteriophage virus.
abstract: The fd bacteriophage is a filamentous virus that is widely used for bio- and nanotechnology applications ranging from phage display to battery materials. The possibility of obtaining a detailed description of its structural properties regardless of its state is therefore essential not only for understanding its physical arrangement and its bacterial infection process but also for many other applications. Here we present a study of the fd phage by magic-angle spinning solid-state NMR. While current structures rely on a Y21M mutant, experiments performed on a strain bearing a wild-type capsid report on high symmetry of the phage and lack of explicit subunit polymorphism. Chemical shift analysis confirmed that the coat protein mostly consists of a rigid right-handed curved α-helix (residues 6-47 of 50), preceded by a flexible loop-structured N-terminus. We were able to qualitatively assign the resonances belonging to the DNA, including the deoxyribose sugars and the thymine bases. These chemical shifts are consistent with base stacking and a C2'-endo/C3'-exo sugar pucker.
authors.affiliation: School of Chemistry, Raymond and Beverly Sackler Faculty of Exact Sciences, Tel Aviv University, Ramat Aviv 69978, Tel Aviv, Israel.
authors.forename: Gili
authors.initials: G
authors.lastname: Abramov
authors.forename: Omry
authors.initials: O
authors.lastname: Morag
authors.forename: Amir
authors.initials: A
authors.lastname: Goldbourt
mesh_terms: D019943:Amino Acid Substitution; D017104:Bacteriophage M13 / Q000378:metabolism*; D036022:Capsid Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004247:DNA / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary
chemical_list: D036022:Capsid Proteins; D004247:DNA