By a News Reporter-Staff News Editor at Proteomics Weekly -- Fresh data on Proteomics are presented in a new report. According to news reporting from Boulder, Colorado, by NewsRx journalists, research stated, "A method was developed to monitor dynamic changes in protein structure and interfacial behavior on surfaces by single-molecule Forster resonance energy transfer. This method entails the incorporation of unnatural amino acids to site-specifically label proteins with single-molecule Forster resonance energy transfer probes for high-throughput dynamic fluorescence tracking microscopy on surfaces."
The news correspondents obtained a quote from the research from the University of Colorado, "Structural changes in the enzyme organophosphorus hydrolase (OPH) were monitored upon adsorption to fused silica (FS) surfaces in the presence of BSA on a molecule-by-molecule basis. Analysis of >30,000 individual trajectories enabled the observation of heterogeneities in the kinetics of surface-induced OPH unfolding with unprecedented resolution. In particular, two distinct pathways were observed: a majority population (similar to 85%) unfolded with a characteristic time scale of 0.10 s, and the remainder unfolded more slowly with a time scale of 0.7 s. Importantly, even after unfolding, OPH readily desorbed from FS surfaces, challenging the common notion that surface-induced unfolding leads to irreversible protein binding. This suggests that protein fouling of surfaces is a highly dynamic process because of subtle differences in the adsorption/desorption rates of folded and unfolded species. Moreover, such observations imply that surfaces may act as a source of unfolded (i.e., aggregation-prone) protein back into solution. Continuing study of other proteins and surfaces will examine whether these conclusions are general or specific to OPH in contact with FS."
According to the news reporters, the research concluded: "Ultimately, this method, which is widely applicable to virtually any protein, provides the framework to develop surfaces and surface modifications with improved biocompatibility."
For more information on this research see: Single-molecule resolution of protein structure and interfacial dynamics on biomaterial surfaces. Proceedings of the National Academy of Sciences of the United States of America, 2013;110(48):19396-19401. 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 S.Y. McLoughlin, University of Colorado, Dept. of Chem & Biol Engn, Boulder, CO 80309, United States. Additional authors for this research include M. Kastantin, D.K. Schwartz and J.L. Kaar (see also Proteomics).
Keywords for this news article include: Boulder, Colorado, Proteomics, United States, Nanotechnology, Protein Structure, Emerging Technologies, North and Central America, Single Molecule Resolution
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