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Insights into virus capsid assembly from non‐covalent mass spectrometry
Author(s) -
Morton Victoria L.,
Stockley Peter G.,
Stonehouse Nicola J.,
Ashcroft Alison E.
Publication year - 2008
Publication title -
mass spectrometry reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 126
eISSN - 1098-2787
pISSN - 0277-7037
DOI - 10.1002/mas.20176
Subject(s) - chemistry , capsid , macromolecule , nanotechnology , mass spectrometry , covalent bond , drug delivery , macromolecular substances , structural biology , function (biology) , biophysics , computational biology , biochemistry , microbiology and biotechnology , materials science , organic chemistry , chromatography , biology , gene
The assembly of viral proteins into a range of macromolecular complexes of strictly defined architecture is one of Nature's wonders. Unraveling the details of these complex structures and the associated self‐assembly pathways that lead to their efficient and precise construction will play an important role in the development of anti‐viral therapeutics. It will also be important in bio‐nanotechnology where there is a plethora of applications for such well‐defined macromolecular complexes, including cell‐specific drug delivery and as substrates for the formation of novel materials with unique electrical and magnetic properties. Mass spectrometry has the ability not only to measure masses accurately but also to provide vital details regarding the composition and stoichiometry of intact, non‐covalently bound macromolecular complexes under near‐physiological conditions. It is thus ideal for exploring the assembly and function of viruses. Over the past decade or so, significant advances have been made in this field, and these advances are summarized in this review, which covers the literature up to the end of 2007. © 2008 Wiley Periodicals, Inc., Mass Spec Rev 27: 575–595, 2008