{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fatima S"],"funding":["Alfred P. Sloan Foundation","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["2040-2050"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11699564"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["63(16)"],"pubmed_abstract":["Hydrogen-bonding (H-bonding) interactions in metalloprotein active sites can critically regulate enzyme function. Changes in the protein structure triggered by interplay with substrates, products, and partner proteins are often translated to the metallocofactor by way of specific changes in H-bond networks connected to the active site. However, the complexities of metalloprotein architecture and mechanism often preclude our ability to define the precise molecular interactions giving rise to these intricate regulatory pathways. To address this shortcoming, we have developed conformationally switchable artificial metalloproteins (swArMs) in which allosteric Gln-binding triggers protein conformational changes that impact the microenvironment surrounding an installed metallocofactor. Herein, w"],"journal":["Biochemistry"],"pubmed_title":["Conformation-Dependent Hydrogen-Bonding Interactions in a Switchable Artificial Metalloprotein."],"pmcid":["PMC11699564"],"funding_grant_id":["R35 GM138138","R24 GM145965","GM138138","R24-GM145965"],"pubmed_authors":["Olshansky L","Bridwell-Rabb J","Boggs DG","Ali N","Fatima S","Singh S","Thielges MC","Aksimentiev A","Mehrafrooz B"],"additional_accession":[]},"is_claimable":false,"name":"Conformation-Dependent Hydrogen-Bonding Interactions in a Switchable Artificial Metalloprotein.","description":"Hydrogen-bonding (H-bonding) interactions in metalloprotein active sites can critically regulate enzyme function. Changes in the protein structure triggered by interplay with substrates, products, and partner proteins are often translated to the metallocofactor by way of specific changes in H-bond networks connected to the active site. However, the complexities of metalloprotein architecture and mechanism often preclude our ability to define the precise molecular interactions giving rise to these intricate regulatory pathways. To address this shortcoming, we have developed conformationally switchable artificial metalloproteins (swArMs) in which allosteric Gln-binding triggers protein conformational changes that impact the microenvironment surrounding an installed metallocofactor. Herein, w","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Aug","modification":"2026-06-01T22:05:18.279Z","creation":"2026-05-22T03:08:21.976Z"},"accession":"S-EPMC11699564","cross_references":{"pubmed":["39088332"],"doi":["10.1021/acs.biochem.4c00209"]}}