By a News Reporter-Staff News Editor at Information Technology Newsweekly -- Researchers detail new data in Bioinformatics. According to news reporting originating in Galveston, Texas, by VerticalNews journalists, research stated, "Owing to the size and complexity of large multi-component biological assemblies, the most tractable approach to determining their atomic structure is often to fit high-resolution radiographic or nuclear magnetic resonance structures of isolated components into lower resolution electron density maps of the larger assembly obtained using cryo-electron microscopy (cryo-EM). This hybrid approach to structure determination requires that an atomic resolution structure of each component, or a suitable homolog, is available."
The news reporters obtained a quote from the research from the University of Texas Medical Branch, "If neither is available, then the amount of structural information regarding that component is limited by the resolution of the cryo-EM map. However, even if a suitable homolog cannot be identified using sequence analysis, a search for structural homologs should still be performed because structural homology often persists throughout evolution even when sequence homology is undetectable, As macromolecules can often be described as a collection of independently folded domains, one way of searching for structural homologs would be to systematically fit representative domain structures from a protein domain database into the medium/low resolution cryo-EM map and return the best fits. Taken together, the best fitting non-overlapping structures would constitute a 'mosaic' backbone model of the assembly that could aid map interpretation and illuminate biological function. Using the computational principles of the Scale-Invariant Feature Transform (SIFT), we have developed FOLD-EM-a computational tool that can identify folded macromolecular domains in medium to low resolution (4-15 A) electron density maps and return a model of the constituent polypeptides in a fully automated fashion."
According to the news reporters, the research concluded: "As a by-product, FOLD-EM can also do flexible multi-domain fitting that may provide insight into conformational changes that occur in macromolecular assemblies."
For more information on this research see: FOLD-EM: automated fold recognition in medium- and low-resolution (4-15 A) electron density maps. Bioinformatics, 2012;28(24):3265-73. Bioinformatics can be contacted at: Oxford Univ Press, Great Clarendon St, Oxford OX2 6DP, England. (Oxford University Press - www.oup.com/; Bioinformatics - bioinformatics.oxfordjournals.org)
Our news correspondents report that additional information may be obtained by contacting M. Saha, Dept. of Biochemistry and Molecular Biology, University of Texas Medical Branch, 301 University Boulevard, Galveston, TX 7555-0647, United States.
The publisher of the journal Bioinformatics can be contacted at: Oxford Univ Press, Great Clarendon St, Oxford OX2 6DP, England.
Keywords for this news article include: Texas, Galveston, United States, Bioinformatics, North and Central America.
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