1ho0

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[[Image:1ho0.jpg|left|200px]]
[[Image:1ho0.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1ho0", creates the "Structure Box" on the page.
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{{STRUCTURE_1ho0| PDB=1ho0 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ho0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ho0 OCA], [http://www.ebi.ac.uk/pdbsum/1ho0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ho0 RCSB]</span>
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'''NEW B-CHAIN MUTANT OF BOVINE INSULIN'''
'''NEW B-CHAIN MUTANT OF BOVINE INSULIN'''
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==About this Structure==
==About this Structure==
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1HO0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HO0 OCA].
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1HO0 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HO0 OCA].
==Reference==
==Reference==
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[[Category: Prigent, Y.]]
[[Category: Prigent, Y.]]
[[Category: Richard, T.]]
[[Category: Richard, T.]]
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[[Category: alpha_helix (9-19)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:03:20 2008''
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[[Category: beta_turn (20-23)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:08:13 2008''
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Revision as of 16:03, 2 May 2008

Template:STRUCTURE 1ho0

NEW B-CHAIN MUTANT OF BOVINE INSULIN


Overview

The solution structure of a new B-chain mutant of bovine insulin, in which the cysteines B7 and B19 are replaced by two serines, has been determined by circular dichroism, 2D-NMR and molecular modeling. This structure is compared with that of the oxidized B-chain of bovine insulin [Hawkins et al. (1995) Int. J. Peptide Protein Res.46, 424-433]. Circular dichroism spectroscopy showed in particular that a higher percentage of helical secondary structure for the B-chain mutant is estimated in trifluoroethanol solution in comparison with the oxidized B-chain. 2D-NMR experiments confirmed, among multiple conformations, that the B-chain mutant presents defined secondary structures such as a alpha-helix between residues B9 and B19, and a beta-turn between amino acids B20 and B23 in aqueous trifluoroethanol. The 3D structures, which are consistent with NMR data and were obtained using a simulated annealing protocol, showed that the tertiary structure of the B-chain mutant is better resolved and is more in agreement with the insulin crystal structure than the oxidized B-chain structure described by Hawkins et al. An explanation could be the presence of two sulfonate groups in the oxidized insulin B-chain. Either by their charges and/or their size, such chemical groups could play a destructuring effect and thus could favor peptide flexibility and conformational averaging. Thus, this study provides new insights on the folding of isolated B-chains.

About this Structure

1HO0 is a Single protein structure. Full crystallographic information is available from OCA.

Reference

A new B-chain mutant of insulin: comparison with the insulin crystal structure and role of sulfonate groups in the B-chain structure., Dupradeau FY, Richard T, Le Flem G, Oulyadi H, Prigent Y, Monti JP, J Pept Res. 2002 Jul;60(1):56-64. PMID:12081626 Page seeded by OCA on Fri May 2 19:03:20 2008

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