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Researchers from University of Cambridge, Medical Research Council Center for Protein Engineering report recent findings in proteomics
May 12th, 2008
2008 MAY 12 -- New investigation results, 'Characterisation of transition state structures for protein folding using 'high', 'medium' and 'low' {Phi}-values,' are detailed in a study published in Protein Engineering, Design & Selection. According to a study from Cambridge, the United Kingdom, "It has been suggested that Phi-values, which allow structural information about transition states (TSs) for protein folding to be obtained, are most reliably interpreted when divided into three classes (high, medium and low). High Phi-values indicate almost completely folded regions in the TS, intermediate Phi-values regions with a detectable amount of structure and low Phi-values indicate mostly unstructured regions." "To explore the extent to which this classification can be used to characterise in detail the structure of TSs for protein folding, we used Phi-values divided into these classes as restraints in molecular dynamics simulations. This type of procedure is related to that used in NMR spectroscopy to define the structure of native proteins from the measurement of inter-proton distances derived from nuclear Overhauser effects. We illustrate this approach by determining the TS ensembles of five proteins and by showing that the results are similar to those obtained by using as restraints the actual numerical Phi-values measured experimentally," wrote C.D. Geierhaas and colleagues, University of Cambridge, Medical Research Council Center for Protein Engineering. The researchers concluded: "Our results indicate that the simultaneous consideration of a set of low-resolution Phi-values can provide sufficient information for characterising the architecture of a TS for folding of a protein." Geierhaas and colleagues published their study in Protein Engineering, Design & Selection (Characterisation of transition state structures for protein folding using 'high', 'medium' and 'low' {Phi}-values. Protein Engineering, Design & Selection, 2008;21(3):215-22). For more information, contact C.D. Geierhaas, University of Cambridge, MRC Centre for Protein Engineering, Cambridge CB2 1EW, UK. Publisher contact information for the journal Protein Engineering, Design & Selection is: Oxford University Press, Great Clarendon St., Oxford OX2 6DP, England. Keywords: United Kingdom, Cambridge, Biotechnology, Medical Device, Protein Engineering, Proteomics. This article was prepared by Proteomics Weekly editors from staff and other reports. Copyright 2008, Proteomics Weekly via NewsRx.com.
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