1orm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1orm.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1orm.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1orm| PDB=1orm | SCENE= }}
{{STRUCTURE_1orm| PDB=1orm | SCENE= }}
-
'''NMR FOLD OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES'''
+
===NMR FOLD OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES===
-
==Overview==
+
<!--
-
The (2)H,(13)C,(15)N-labeled, 148-residue integral membrane protein OmpX from Escherichia coli was reconstituted with dihexanoyl phosphatidylcholine (DHPC) in mixed micelles of molecular mass of about 60 kDa. Transverse relaxation-optimized spectroscopy (TROSY)-type triple resonance NMR experiments and TROSY-type nuclear Overhauser enhancement spectra were recorded in 2 mM aqueous solutions of these mixed micelles at pH 6.8 and 30 degrees C. Complete sequence-specific NMR assignments for the polypeptide backbone thus have been obtained. The (13)C chemical shifts and the nuclear Overhauser effect data then resulted in the identification of the regular secondary structure elements of OmpX/DHPC in solution and in the collection of an input of conformational constraints for the computation of the global fold of the protein. The same type of polypeptide backbone fold is observed in the presently determined solution structure and the previously reported crystal structure of OmpX determined in the presence of the detergent n-octyltetraoxyethylene. Further structure refinement will have to rely on the additional resonance assignment of partially or fully protonated amino acid side chains, but the present data already demonstrate that relaxation-optimized NMR techniques open novel avenues for studies of structure and function of integral membrane proteins.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11226244}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11226244 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11226244}}
==About this Structure==
==About this Structure==
-
1ORM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORM OCA].
+
1ORM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORM OCA].
==Reference==
==Reference==
Line 33: Line 37:
[[Category: Ompx]]
[[Category: Ompx]]
[[Category: Trosy]]
[[Category: Trosy]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:11:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:13:59 2008''

Revision as of 01:14, 28 July 2008

Image:1orm.png

Template:STRUCTURE 1orm

NMR FOLD OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES

Template:ABSTRACT PUBMED 11226244

About this Structure

1ORM is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles., Fernandez C, Adeishvili K, Wuthrich K, Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2358-63. Epub 2001 Feb 20. PMID:11226244

Page seeded by OCA on Mon Jul 28 04:13:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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