1fh1
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(New page: 200px<br /><applet load="1fh1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fh1" /> '''BACKBONE FOLD OF NODF'''<br /> ==Overview==...)
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Revision as of 12:48, 20 November 2007
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BACKBONE FOLD OF NODF
Overview
Over the next few years, various genome projects will sequence many new, genes and yield many new gene products. Many of these products will have, no known function and little, if any, sequence homology to existing, proteins. There is reason to believe that a rapid determination of a, protein fold, even at low resolution, can aid in the identification of, function and expedite the determination of structure at higher resolution., Recently devised NMR methods of measuring residual dipolar couplings, provide one route to the determination of a fold. They do this by allowing, the alignment of previously identified secondary structural elements with, respect to each other. When combined with constraints involving loops, connecting elements or other short-range experimental distance, information, a fold is produced. We illustrate this approach to protein, fold determination on (15)N-labeled Eschericia coli acyl carrier protein, using a limited set of (15)N-(1)H and (1)H-(1)H dipolar couplings. We also, illustrate an approach using a more extended set of heteronuclear, couplings on a related protein, (13)C, (15)N-labeled NodF protein from, Rhizobium leguminosarum.
About this Structure
1FH1 is a Single protein structure of sequence from Rhizobium leguminosarum. Full crystallographic information is available from OCA.
Reference
Rapid determination of protein folds using residual dipolar couplings., Fowler CA, Tian F, Al-Hashimi HM, Prestegard JH, J Mol Biol. 2000 Dec 1;304(3):447-60. PMID:11090286
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