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1gjz

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{{STRUCTURE_1gjz| PDB=1gjz | SCENE= }}
{{STRUCTURE_1gjz| PDB=1gjz | SCENE= }}
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'''SOLUTION STRUCTURE OF A DIMERIC N-TERMINAL FRAGMENT OF HUMAN UBIQUITIN'''
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===SOLUTION STRUCTURE OF A DIMERIC N-TERMINAL FRAGMENT OF HUMAN UBIQUITIN===
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==Overview==
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Previous peptide dissection and kinetic experiments have indicated that in vitro folding of ubiquitin may proceed via transient species in which native-like structure has been acquired in the first 45 residues. A peptide fragment, UQ(1-51), encompassing residues 1 to 51 of ubiquitin was produced in order to test whether this portion has propensity for independent self-assembly. Surprisingly, the construct formed a folded symmetrical dimer that was stabilised by 0.8 M sodium sulphate at 298 K (the S state). The solution structure of the UQ(1-51) dimer was determined by multinuclear NMR spectroscopy. Each subunit of UQ(1-51) consists of an N-terminal beta-hairpin followed by an alpha-helix and a final beta-strand, with orientations similar to intact ubiquitin. The dimer is formed by the third beta-strand of one subunit interleaving between the hairpin and third strand of the other to give a six-stranded beta-sheet, with the two alpha-helices sitting on top. The helix-helix and strand portions of the dimer interface also mimic related features in the structure of ubiquitin. The structural specificity of the UQ(1-51) peptide is tuneable: as the concentration of sodium sulphate is decreased, near-native alternative conformations are populated in slow chemical exchange. Magnetization transfer experiments were performed to characterize the various species present in 0.35 M sodium sulphate, namely the S state and two minor forms. Chemical shift differences suggest that one minor form is very similar to the S state, while the other experiences a significant conformational change in the third strand. A segmental rearrangement of the third strand in one subunit of the S state would render the dimer asymmetric, accounting for most of our results. Similar small-scale transitions in proteins are often invoked to explain solvent exchange at backbone amide proton sites that have an intermediate level of protection.
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(as it appears on PubMed at http://www.pubmed.gov), where 11733996 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11733996}}
==About this Structure==
==About this Structure==
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1GJZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJZ OCA].
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1GJZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJZ OCA].
==Reference==
==Reference==
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[[Category: Protein dissection]]
[[Category: Protein dissection]]
[[Category: Ubiquitin]]
[[Category: Ubiquitin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:40:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:24:58 2008''

Revision as of 02:25, 1 July 2008

Image:1gjz.png

Template:STRUCTURE 1gjz

SOLUTION STRUCTURE OF A DIMERIC N-TERMINAL FRAGMENT OF HUMAN UBIQUITIN

Template:ABSTRACT PUBMED 11733996

About this Structure

1GJZ is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Structure and properties of a dimeric N-terminal fragment of human ubiquitin., Bolton D, Evans PA, Stott K, Broadhurst RW, J Mol Biol. 2001 Dec 7;314(4):773-87. PMID:11733996

Page seeded by OCA on Tue Jul 1 05:24:58 2008

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