<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Dinakarpandian D</submitter><funding>NIBIB NIH HHS</funding><pagination>2</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC539358</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>4(1)</volume><pubmed_abstract>BACKGROUND: The amino acid composition of a low molecular weight chromium binding peptide (LMWCr), isolated from bovine liver, is reportedly E:G:C:D::4:2:2:2, though its sequence has not been discovered. There is some controversy surrounding the exact biochemical forms and the action of Cr(III) in biological systems; the topic has been the subject of many experimental reports and continues to be investigated. Clarification of Cr-protein interactions will further understanding Cr(III) biochemistry and provide a basis for novel therapies based on metallocomplexes or small molecules. RESULTS: A genomic search of the non-redundant database for all possible decapeptides of the reported composition yields three exact matches, EDGEECDCGE, DGEECDCGEE and CEGGCEEDDE. The first two sequences are fou</pubmed_abstract><journal>BMC chemical biology</journal><pubmed_title>An informatics search for the low-molecular weight chromium-binding peptide.</pubmed_title><pmcid>PMC539358</pmcid><funding_grant_id>P41 EB001980</funding_grant_id><pubmed_authors>Van Horn JD</pubmed_authors><pubmed_authors>Amini K</pubmed_authors><pubmed_authors>Chaudhary S</pubmed_authors><pubmed_authors>Bennett B</pubmed_authors><pubmed_authors>Dinakarpandian D</pubmed_authors><pubmed_authors>Morrissette V</pubmed_authors></additional><is_claimable>false</is_claimable><name>An informatics search for the low-molecular weight chromium-binding peptide.</name><description>BACKGROUND: The amino acid composition of a low molecular weight chromium binding peptide (LMWCr), isolated from bovine liver, is reportedly E:G:C:D::4:2:2:2, though its sequence has not been discovered. There is some controversy surrounding the exact biochemical forms and the action of Cr(III) in biological systems; the topic has been the subject of many experimental reports and continues to be investigated. Clarification of Cr-protein interactions will further understanding Cr(III) biochemistry and provide a basis for novel therapies based on metallocomplexes or small molecules. RESULTS: A genomic search of the non-redundant database for all possible decapeptides of the reported composition yields three exact matches, EDGEECDCGE, DGEECDCGEE and CEGGCEEDDE. The first two sequences are fou</description><dates><release>2004-01-01T00:00:00Z</release><publication>2004 Dec</publication><modification>2026-05-03T18:48:22.286Z</modification><creation>2019-03-27T01:08:26Z</creation></dates><accession>S-EPMC539358</accession><cross_references><pubmed>15603587</pubmed><doi>10.1186/1472-6769-4-2</doi></cross_references></HashMap>