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Follow on Google News | New Insights Published on Key Protein Interactions Involved in the Bacterial FlagellarNew Application Note from Wyatt Technology Showcases the Ability of CG-MALS to Quantify Complex Proteins
By: Wyatt Technology The application note demonstrates how the use of the Calypso® II composition- In the first part of the analysis, the binding affinity between FliM and the two FliG domains (FliGM and FliGC) were measured individually. The results demonstrate a 100-fold difference in binding affinity between FliGM (KD = 6.6 μM) and FliGC (KD = 580 μM) for FliM. This large difference in affinity supports the current hypothesis for switching the rotational direction of the flagella: The tighter-binding FliGM domain remains bound while the weaker-binding FliGc domain can be displaced by other regulatory proteins to change the direction of rotation. When the binding between FliM and full-length FliG was tested, a slow, time-dependent association into large complexes was observed. This large association was hinted at by previous NMR studies but could not be quantified by this technique. Measuring the molar mass as a function of time by CG-MALS provides direction for future studies and may help determine the mechanism of flagellar motor switching. With this application note, Wyatt Technology demonstrates how CG-MALS provided invaluable information about the complex interactions between the proteins involved in the bacterial flagellar motor switching mechanism. Sophia Kenrick from Wyatt Technology explains, “CG-MALS provides new data explaining the binding of FliG to FliM, which could not have been obtained by other methods. The same CG-MALS technique used to investigate the structure-function relationship of the flagellar proteins can be extended to other complex protein assemblies, such as the large microchannels bacteria and other pathogens use to inject toxins into a host. Understanding how the proteins work together may help with research into how to disrupt these interactions and control the spread of these pathogens.” The Calypso II combined with a DAWN HELEOS or miniDAWN® TREOS® MALS detector encompass a complete composition- To learn more about Wyatt Technology, please visit www.wyatt.com (http://bit.ly/ About Wyatt Based in Santa Barbara, California, Wyatt Technology is the world’s leading provider of instruments for absolute macromolecular and nanoparticle characterization. With over 40 years’ experience developing multi-angle light scattering detectors, working with customers in the biotechnology, chemical, petrochemical, pharmaceutical, academic and government arenas, Wyatt prides itself on its entrepreneurial spirit, and the uniqueness of its offerings. The Company’s groundbreaking technology and uncompromising levels of customer care make Wyatt the global hallmark in its field. For more information, please visit www.wyatt.com (http://bit.ly/ For further press information please contact: Sarah Morley, The Scott Partnership, 1, Whiteside, Station Road, Holmes Chapel, Cheshire, CW4 8AA, United Kingdom Tel: + 44 1477 539539 Fax: +44 1477 539540 email to:wyatt@scottpr.com End
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