1omt
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(New page: 200px<br /><applet load="1omt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1omt" /> '''SOLUTION STRUCTURE OF OVOMUCOID (THIRD DOMAI...)
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Revision as of 20:53, 20 November 2007
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SOLUTION STRUCTURE OF OVOMUCOID (THIRD DOMAIN) FROM DOMESTIC TURKEY (298K, PH 4.1) (NMR, 50 STRUCTURES) (STANDARD NOESY ANALYSIS)
Overview
Network-editing experiments are variants of the basic NOESY experiment, that allow more accurate direct measurement of interproton distances in, macromolecules by defeating specific spin-diffusion pathways. Two, network-editing approaches, block-decoupled NOESY and, complementary-block-decoupled-NOESY, were applied as three-dimensional, heteronuclear-edited experiments to distance measurement in a small, protein, turkey ovomucoid third domain (OMTKY3). Two-hundred and twelve of, the original 655 distance constraints observed in this molecule (Krezel AM, et al., 1994, J Mol Biol 242:203-214) were improved by their replacement, by distances derived from network-edited spectra, and distance, geometry/simulated annealing solution structure calculations were, performed from both the unimproved and improved distance sets. The, resulting two families of structures were found to differ significantly, the most important differences being the hinge angle of a beta-turn and an, expansion of the sampled conformation space in the region of the, reactive-site loop. The structures calculated from network-editing data, are interpreted as a more accurate model of the solution conformation of, OMTKY3.
About this Structure
1OMT is a Single protein structure of sequence from Meleagris gallopavo. Full crystallographic information is available from OCA.
Reference
Comparison of the accuracy of protein solution structures derived from conventional and network-edited NOESY data., Hoogstraten CG, Choe S, Westler WM, Markley JL, Protein Sci. 1995 Nov;4(11):2289-99. PMID:8563625
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