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.
%0 Journal Article
%1 opella_structure_2008
%A Opella, Stanley J
%A Zeri, Ana Carolina
%A Park, Sang Ho
%D 2008
%J Annu Rev Phys Chem
%K Animals,Bacteriophages,Biology,Capsid Internalization Library,Virus Proteins,Magnetic Resonance Spectroscopy,Peptide
%P 635--657
%R 10.1146/annurev.physchem.58.032806.104640
%T Structure, dynamics, and assembly of filamentous bacteriophages by nuclear magnetic resonance spectroscopy
%V 59
%X 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.
@article{opella_structure_2008,
abstract = {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.},
added-at = {2017-03-14T02:48:56.000+0100},
author = {Opella, Stanley J and Zeri, Ana Carolina and Park, Sang Ho},
biburl = {https://www.bibsonomy.org/bibtex/241d15e4b90e011426c326b82fcd764b8/nmrresource},
doi = {10.1146/annurev.physchem.58.032806.104640},
interhash = {85c5c83cfaa1ee12bda68b4ce6543330},
intrahash = {41d15e4b90e011426c326b82fcd764b8},
issn = {0066-426X},
journal = {Annu Rev Phys Chem},
keywords = {Animals,Bacteriophages,Biology,Capsid Internalization Library,Virus Proteins,Magnetic Resonance Spectroscopy,Peptide},
pages = {635--657},
pmid = {18393681},
timestamp = {2017-03-14T02:49:21.000+0100},
title = {{Structure, dynamics, and assembly of filamentous bacteriophages by nuclear magnetic resonance spectroscopy}},
volume = 59,
year = 2008
}