1omt
From Proteopedia
(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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| - | [[Image:1omt.gif|left|200px]]<br /><applet load="1omt" size=" | + | [[Image:1omt.gif|left|200px]]<br /><applet load="1omt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1omt" /> | caption="1omt" /> | ||
'''SOLUTION STRUCTURE OF OVOMUCOID (THIRD DOMAIN) FROM DOMESTIC TURKEY (298K, PH 4.1) (NMR, 50 STRUCTURES) (STANDARD NOESY ANALYSIS)'''<br /> | '''SOLUTION STRUCTURE OF OVOMUCOID (THIRD DOMAIN) FROM DOMESTIC TURKEY (298K, PH 4.1) (NMR, 50 STRUCTURES) (STANDARD NOESY ANALYSIS)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Network-editing experiments are variants of the basic NOESY experiment | + | 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== | ==About this Structure== | ||
| - | 1OMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http:// | + | 1OMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Choe, S.]] | [[Category: Choe, S.]] | ||
| - | [[Category: Hoogstraten, C | + | [[Category: Hoogstraten, C G.]] |
| - | [[Category: Markley, J | + | [[Category: Markley, J L.]] |
| - | [[Category: Westler, W | + | [[Category: Westler, W M.]] |
[[Category: bd-noesy]] | [[Category: bd-noesy]] | ||
[[Category: cbd-noesy]] | [[Category: cbd-noesy]] | ||
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[[Category: spin diffusion]] | [[Category: spin diffusion]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:24 2008'' |
Revision as of 12:19, 21 February 2008
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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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