Structure, dynamics, and assembly of filamentous bacteriophages by nuclear magnetic resonance spectroscopy.
Filamentous bacteriophages serve as model systems for the development and implementation of spectroscopic methods suitable for biological supramolecular assemblies. Not only are their coat proteins small and readily prepared in the laboratory, but they also have two primary roles as membrane proteins and as the principal structural element of the virus particles. As a bacterial system, they are readily labeled with stable isotopes, and this has opened possibilities for the many nuclear magnetic resonance (NMR) studies described in this review. In particular, solid-state NMR of aligned samples has been used to determine the three-dimensional structures of both the membrane-bound forms of coat proteins in phospholipid bilayers and structural forms in virus particles, which has led to an analysis of the assembly mechanism for virus particles as they are extruded through the cell membrane.
Opella
Stanley J
SJ
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093, USA. sopella@ucsd.edu
Zeri
Ana Carolina
AC
Park
Sang Ho
SH
D000818:Animals; D001435:Bacteriophages / Q000737:chemistry* / Q000378:metabolism; D001695:Biology; D036022:Capsid Proteins / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D019151:Peptide Library; D053586:Virus Internalization
D036022:Capsid Proteins; D019151:Peptide Library