{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["LeMaster DM"],"funding":["NIGMS NIH HHS"],"pagination":["81"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2249605"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7"],"pubmed_abstract":["<h4>Background</h4>Chimeric hybrids derived from the rubredoxins of Pyrococcus furiosus (Pf) and Clostridium pasteurianum (Cp) provide a robust system for the characterization of protein conformational stability and dynamics in a differential mode. Interchange of the seven nonconserved residues of the metal binding site between the Pf and Cp rubredoxins yields a complementary pair of hybrids, for which the sum of the thermodynamic stabilities is equal to the sum for the parental proteins. Furthermore, the increase in amide hydrogen exchange rates for the hyperthermophile-derived metal binding site hybrid is faithfully mirrored by a corresponding decrease for the complementary hybrid that is derived from the less thermostable rubredoxin, indicating a degree of additivity in the conformation"],"journal":["BMC structural biology"],"pubmed_title":["NMR and X-ray analysis of structural additivity in metal binding site-swapped hybrids of rubredoxin."],"pmcid":["PMC2249605"],"funding_grant_id":["R01 GM064736","GM 64736"],"pubmed_authors":["Li H","Hernandez G","Guo Y","LeMaster DM","Anderson JS","Wang L"],"additional_accession":[]},"is_claimable":false,"name":"NMR and X-ray analysis of structural additivity in metal binding site-swapped hybrids of rubredoxin.","description":"<h4>Background</h4>Chimeric hybrids derived from the rubredoxins of Pyrococcus furiosus (Pf) and Clostridium pasteurianum (Cp) provide a robust system for the characterization of protein conformational stability and dynamics in a differential mode. Interchange of the seven nonconserved residues of the metal binding site between the Pf and Cp rubredoxins yields a complementary pair of hybrids, for which the sum of the thermodynamic stabilities is equal to the sum for the parental proteins. Furthermore, the increase in amide hydrogen exchange rates for the hyperthermophile-derived metal binding site hybrid is faithfully mirrored by a corresponding decrease for the complementary hybrid that is derived from the less thermostable rubredoxin, indicating a degree of additivity in the conformation","dates":{"release":"2007-01-01T00:00:00Z","publication":"2007 Dec","modification":"2025-05-29T20:33:05.344Z","creation":"2019-03-27T00:13:54Z"},"accession":"S-EPMC2249605","cross_references":{"pubmed":["18053245"],"doi":["10.1186/1472-6807-7-81"]}}