{"doi":"10.1063/1.5130582","title":"Conformational sampling and kinetics changes across a non-Arrhenius break point in the enzyme thermolysin","abstract":"Numerous studies have suggested a significant role that protein dynamics play in optimizing enzyme catalysis, and changes in conformational sampling offer a window to explore this role. Thermolysin from Bacillus thermoproteolyticus rokko, which is a heat-stable zinc metalloproteinase, serves here as a model system to study changes of protein function and conformational sampling across a temperature range of 16–36 °C. The temperature dependence of kinetics of thermolysin showed a biphasic transition at 26 °C that points to potential conformational and dynamic differences across this temperature. The non-Arrhenius behavior observed resembled results from previous studies of a thermophilic alcohol dehydrogenase enzyme, which also indicated a biphasic transition at ambient temperatures. To explore the non-Arrhenius behavior of thermolysin, room temperature crystallography was applied to characterize structural changes in a temperature range across the biphasic transition temperature. The alternate conformation of side chain fitting to electron density of a group of residues showed a higher variability in the temperature range from 26 to 29 °C, which indicated a change in conformational sampling that correlated with the non-Arrhenius break point.","journal":"Structural Dynamics","year":2020,"id":89756,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":8,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":0.9462,"is_data_producer":false,"deposit_databanks":null,"is_oa":true,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":"2020-01-01","fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":453295,"name":"Mackenzie L. Lauro","orcid":"0000-0002-0041-6562","position":1,"is_corresponding":false},{"id":454126,"name":"Timothy J. Koblish","orcid":null,"position":2,"is_corresponding":false},{"id":453296,"name":"Brian J. Bahnson","orcid":"0000-0002-1562-8314","position":3,"is_corresponding":false},{"id":369461,"name":"Ming Dong","orcid":"0000-0002-9121-6020","position":0,"is_corresponding":true}],"reference_count":38,"raw_metadata":null,"created_at":"2026-07-18T22:02:27.195966Z","pmid":"32095489","pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}