{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Li H"],"funding":["European Research Council","NIGMS NIH HHS","Engineering and Physical Sciences Research Council"],"pagination":["1269-79"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3631356"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["21(9)"],"pubmed_abstract":["Chemical crosslinking in combination with Fourier transform ion cyclotron resonance mass spectrometry (FTICR MS) has significant potential for studying protein structures and protein-protein interactions. Previously, cisplatin has been shown to be a crosslinker and crosslinks multiple methionine (Met) residues in apo-calmodulin (apo-CaM). However, the inter-residue distances obtained from nuclear magnetic resonance structures are inconsistent with the measured distance constraints by crosslinking. Met residues lie too far apart to be crosslinked by cisplatin. Here, by combining FTICR MS with a novel computational flexibility analysis, the flexible nature of the CaM structure is found to be key to cisplatin crosslinking in CaM. It is found that the side chains of Met residues can be brought"],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["Protein flexibility is key to cisplatin crosslinking in calmodulin."],"pmcid":["PMC3631356"],"funding_grant_id":["EP/F034210/1","247450","EP/G006792/1","R01GM078293","R01 GM078293"],"pubmed_authors":["Li H","Wells SA","Romer RA","Sadler PJ","Jimenez-Roldan JE","O'Connor PB","Zhao Y"],"additional_accession":[]},"is_claimable":false,"name":"Protein flexibility is key to cisplatin crosslinking in calmodulin.","description":"Chemical crosslinking in combination with Fourier transform ion cyclotron resonance mass spectrometry (FTICR MS) has significant potential for studying protein structures and protein-protein interactions. Previously, cisplatin has been shown to be a crosslinker and crosslinks multiple methionine (Met) residues in apo-calmodulin (apo-CaM). However, the inter-residue distances obtained from nuclear magnetic resonance structures are inconsistent with the measured distance constraints by crosslinking. Met residues lie too far apart to be crosslinked by cisplatin. Here, by combining FTICR MS with a novel computational flexibility analysis, the flexible nature of the CaM structure is found to be key to cisplatin crosslinking in CaM. It is found that the side chains of Met residues can be brought","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Sep","modification":"2026-05-01T06:36:55.348Z","creation":"2019-03-27T01:07:40Z"},"accession":"S-EPMC3631356","cross_references":{"pubmed":["22733664"],"doi":["10.1002/pro.2111"]}}