1ho0

<StructureSection load='1ho0' size='340' side='right'caption='[[1ho0]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1ho0]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HO0 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ho0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ho0 OCA], [https://pdbe.org/1ho0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ho0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ho0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ho0 ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/INS_BOVIN INS_BOVIN]] Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:12081626</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Dupradeau, F Y]]

[[Category: Flem, G Le]]

[[Category: Monti, J P]]

[[Category: Oulyadi, H]]

[[Category: Prigent, Y]]

[[Category: Richard, T]]

[[Category: Hormone-growth factor complex]]