1omt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1omt.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1omt.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1omt| PDB=1omt | SCENE= }}
{{STRUCTURE_1omt| PDB=1omt | SCENE= }}
-
'''SOLUTION STRUCTURE OF OVOMUCOID (THIRD DOMAIN) FROM DOMESTIC TURKEY (298K, PH 4.1) (NMR, 50 STRUCTURES) (STANDARD NOESY ANALYSIS)'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8563625}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8563625 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8563625}}
==About this Structure==
==About this Structure==
-
1OMT is a [[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].
+
1OMT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMT OCA].
==Reference==
==Reference==
Line 30: Line 34:
[[Category: Network editing]]
[[Category: Network editing]]
[[Category: Spin diffusion]]
[[Category: Spin diffusion]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:02:33 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:51:24 2008''

Revision as of 03:51, 28 July 2008

Image:1omt.png

Template:STRUCTURE 1omt

SOLUTION STRUCTURE OF OVOMUCOID (THIRD DOMAIN) FROM DOMESTIC TURKEY (298K, PH 4.1) (NMR, 50 STRUCTURES) (STANDARD NOESY ANALYSIS)

Template:ABSTRACT PUBMED 8563625

About this Structure

1OMT is a Single protein structure of sequence from Meleagris gallopavo. Full experimental 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

Page seeded by OCA on Mon Jul 28 06:51:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1omt"
Personal tools