1egs: Difference between revisions

Revision as of 00:40, 1 July 2008

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File:1egs.png

Template:STRUCTURE 1egs

NMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETIC PEPTIDE (RESIDUES 13-32) BOUND TO GROEL, 20 STRUCTURESNMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETIC PEPTIDE (RESIDUES 13-32) BOUND TO GROEL, 20 STRUCTURES

Template:ABSTRACT PUBMED 8876186

About this StructureAbout this Structure

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

ReferenceReference

Interplay of structure and disorder in cochaperonin mobile loops., Landry SJ, Taher A, Georgopoulos C, van der Vies SM, Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11622-7. PMID:8876186

Page seeded by OCA on Tue Jul 1 00:40:34 2008

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OCA

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-'''NMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETIC PEPTIDE (RESIDUES 13-32) BOUND TO GROEL, 20 STRUCTURES'''
+===NMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETIC PEPTIDE (RESIDUES 13-32) BOUND TO GROEL, 20 STRUCTURES===
-==Overview==
+<!--
-Protein-protein interactions typically are characterized by highly specific interfaces that mediate binding with precisely tuned affinities. Binding of the Escherichia coli cochaperonin GroES to chaperonin GroEL is mediated, at least in part, by a mobile polypeptide loop in GroES that becomes immobilized in the GroEL/GroES/nucleotide complex. The bacteriophage T4 cochaperonin Gp31 possesses a similar highly flexible polypeptide loop in a region of the protein that shows low, but significant, amino acid similarity with GroES and other cochaperonins. When bound to GroEL, a synthetic peptide representing the mobile loop of either GroES or Gp31 adopts a characteristic bulged hairpin conformation as determined by transferred nuclear Overhauser effects in NMR spectra. Thermodynamic considerations suggest that flexible disorder in the cochaperonin mobile loops moderates their affinity for GroEL to facilitate cycles of chaperonin-mediated protein folding.
+The line below this paragraph, {{ABSTRACT_PUBMED_8876186}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_8876186}}
 ==About this Structure==
-EGS 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=1EGS OCA].
+EGS 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=1EGS OCA].
 ==Reference==
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 [[Category: Nmr]]
 [[Category: Protein folding]]
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