From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1ho0.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1ho0.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1ho0| PDB=1ho0 | SCENE= }} | | {{STRUCTURE_1ho0| PDB=1ho0 | SCENE= }} |
| | | | |
| - | '''NEW B-CHAIN MUTANT OF BOVINE INSULIN'''
| + | ===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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_12081626}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12081626 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_12081626}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| - | 1HO0 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HO0 OCA]. | + | 1HO0 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HO0 OCA]. |
| | | | |
| | ==Reference== | | ==Reference== |
| Line 27: |
Line 31: |
| | [[Category: Prigent, Y.]] | | [[Category: Prigent, Y.]] |
| | [[Category: Richard, T.]] | | [[Category: Richard, T.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:03:20 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:27:11 2008'' |
Revision as of 05:27, 1 July 2008
Template:STRUCTURE 1ho0
NEW B-CHAIN MUTANT OF BOVINE INSULIN
Template:ABSTRACT PUBMED 12081626
About this Structure
1HO0 is a Single protein structure. Full experimental 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 Tue Jul 1 08:27:11 2008
