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10.1002/mas.20176 http://scihub22266oqcxt.onion/10.1002/mas.20176 18498137!7168407!18498137     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Mass+Spectrom+Rev 2008 ; 27 (6): 575-95 Nephropedia Template TP {{tp|p=18498137|t=2008. Insights into virus capsid assembly from non-covalent mass spectrometry |pdf=|usr=}}{{18498137}} gab.com Text Insights into virus capsid assembly from non-covalent mass spectrometry JO: Mass Spectrom Rev http://www.kidney.de/pget.php?&tw=1&pmid=18498137 #FOAvip 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. Twit Text FOAVip Insights into virus capsid assembly from non-covalent mass spectrometry ????Mass Spectrom Rev http://www.kidney.de/pget.php?&tw=1&pmid=18498137 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=18498137 #FOAvip English Wikipedia <ref>{{Cite pmid|18498137}}</ref> Insights into virus capsid assembly from non-covalent mass spectrometry #MMPMID18498137 Morton VL; Stockley PG; Stonehouse NJ; Ashcroft AE Mass Spectrom Rev 2008[Nov]; 27 (6): 575-95 PMID18498137show ga 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. |Capsid Proteins/*chemistry/*metabolism[MESH] |Capsid/*chemistry/*physiology[MESH] |Mass Spectrometry/*methods[MESH]Insights into virus capsid assembly from non-covalent mass spectrometr(epmc).pdf DeepDyve Pubget Overpricing