1qgm: Difference between revisions

Revision as of 22:59, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1qgm.png

Template:STRUCTURE 1qgm

THE SOLUTION STRUCTURE OF A 30 RESIDUE AMINO-TERMINAL DOMAIN OF THE CARP GRANULIN-1 PROTEIN.THE SOLUTION STRUCTURE OF A 30 RESIDUE AMINO-TERMINAL DOMAIN OF THE CARP GRANULIN-1 PROTEIN.

Template:ABSTRACT PUBMED 10424355

About this StructureAbout this Structure

1QGM is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

A 30-residue fragment of the carp granulin-1 protein folds into a stack of two beta-hairpins similar to that found in the native protein., Vranken WF, Chen ZG, Xu P, James S, Bennett HP, Ni F, J Pept Res. 1999 May;53(5):590-7. PMID:10424355

Page seeded by OCA on Mon Jul 28 22:59:54 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1qgm.jpg|left|200px]]
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 {{STRUCTURE_1qgm|  PDB=1qgm  |  SCENE=  }}
-'''THE SOLUTION STRUCTURE OF A 30 RESIDUE AMINO-TERMINAL DOMAIN OF THE CARP GRANULIN-1 PROTEIN.'''
+===THE SOLUTION STRUCTURE OF A 30 RESIDUE AMINO-TERMINAL DOMAIN OF THE CARP GRANULIN-1 PROTEIN.===
-==Overview==
+<!--
-Upon air oxidation, a peptide corresponding to the 30-residue N-terminal subdomain of carp granulin-1 spontaneously formed the disulfide pairing observed in the native protein. Structural characterization using NMR showed the presence of a defined secondary structure within this peptide. The chemical shifts for most of the alphaCH protons of the peptide and the protein are very similar, and the observed NOE contacts of the peptide strongly resemble those in the protein. A structure calculation of the peptide using NOE distance constraints indicates that the peptide fragment adopts the same conformation as formed within the native protein. The 30-residue N-terminal peptide of carp granulin-1 is the first example of an independently folded stack of two beta-hairpins reinforced by two interhairpin disulfide bonds. Two key areas of the structure show a clustering of hydrophobic residues that may account for its exceptional conformational stability.
+The line below this paragraph, {{ABSTRACT_PUBMED_10424355}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10424355 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10424355}}
 ==About this Structure==
-QGM is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QGM OCA].
+QGM is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QGM OCA].
 ==Reference==
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 [[Category: Beta-hairpin stack]]
 [[Category: Conformational stability]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:14:45 2008''
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