1qgm: Difference between revisions
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[[ | ==THE SOLUTION STRUCTURE OF A 30 RESIDUE AMINO-TERMINAL DOMAIN OF THE CARP GRANULIN-1 PROTEIN.== | ||
<StructureSection load='1qgm' size='340' side='right' caption='[[1qgm]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1qgm]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QGM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QGM FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qgm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qgm RCSB], [http://www.ebi.ac.uk/pdbsum/1qgm PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:10424355</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Ni, F.]] | [[Category: Ni, F.]] | ||
[[Category: Vranken, W F.]] | [[Category: Vranken, W F.]] | ||
Revision as of 11:29, 8 October 2014
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.
Structural highlights
Publication Abstract from PubMedUpon 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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