By a News Reporter-Staff News Editor at Science Letter -- Current study results on Morbillivirus Infections have been published. According to news reporting out of Stony Brook, New York, by NewsRx editors, research stated, "Numerous relatively short regions within intrinsically disordered proteins (IDPs) serve as molecular recognition elements (MoREs). They fold into ordered structures upon binding to their partner molecules."
Our news journalists obtained a quote from the research from the State University of New York, "Currently, there is still a lack of in-depth understanding of how coupled binding and folding occurs in MoREs. Here, we quantified the unbound ensembles of the alpha-MoRE within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein. We developed a multiscaled approach by combining a physics-based and an atomic hybrid model to decipher the mechanism by which the alpha-MoRE interacts with the X domain of the measles virus phosphoprotein. Our multiscaled approach led to remarkable qualitative and quantitative agreements between the theoretical predictions and experimental results (e.g., chemical shifts). We found that the free alpha-MoRE rapidly interconverts between multiple discrete partially helical conformations and the unfolded state, in accordance with the experimental observations. We quantified the underlying global folding-binding landscape. This leads to a synergistic mechanism in which the recognition event proceeds via (minor) conformational selection, followed by (major) induced folding. We also provided evidence that the alpha-MoRE is a compact molten globule-like IDP and behaves as a downhill folder in the induced folding process. We further provided a theoretical explanation for the inherent connections between 'downhill folding,' 'molten globule,' and 'intrinsic disorder' in IDP-related systems."
According to the news editors, the research concluded: "Particularly, we proposed that binding and unbinding of IDPs proceed in a stepwise way through a 'kinetic divide-and-conquer' strategy that confers them high specificity without high affinity."
For more information on this research see: Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein. Proceedings of the National Academy of Sciences of the United States of America, 2013;110(40):E3743-E3752. Proceedings of the National Academy of Sciences of the United States of America can be contacted at: Natl Acad Sciences, 2101 Constitution Ave NW, Washington, DC 20418, USA. (National Academy of Sciences - www.nasonline.org/; Proceedings of the National Academy of Sciences of the United States of America - www.nasonline.org/publications/pnas/)
Our news journalists report that additional information may be obtained by contacting Y. Wang, SUNY Stony Brook, Dept. of Chem & Phys, Stony Brook, NY 11794, United States. Additional authors for this research include X.K. Chu, S. Longhi, P. Roche, W. Han, E.K. Wang and J. Wang (see also Morbillivirus Infections).
Keywords for this news article include: New York, Virology, Stony Brook, RNA Viruses, United States, Measles Virus, Nanotechnology, Nucleoproteins, Mononegavirales, Paramyxovirinae, Emerging Technologies, Molecular Recognition, Morbillivirus Infections, North and Central America, Paramyxoviridae Infections
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