{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Xi K"],"funding":["Warshel Institute for Computational Biology","National Science Foundation of China","Shenzhen Fundamental Research Fund","Shenzhen-Hong Kong Cooperation Zone for Technology and Innovation","the National Science Foundation of China"],"pagination":["14628"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9736071"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(23)"],"pubmed_abstract":["Bacteriophage T4 lysozyme (T4L) is a glycosidase that is widely applied as a natural antimicrobial agent in the food industry. Due to its wide applications and small size, T4L has been regarded as a model system for understanding protein dynamics and for large-scale protein engineering. Through structural insights from the single conformation of T4L, a series of mutations (L99A,G113A,R119P) have been introduced, which have successfully raised the fractional population of its only hydrolysis-competent excited state to 96%. However, the actual impact of these substitutions on its dynamics remains unclear, largely due to the lack of highly efficient sampling algorithms. Here, using our recently developed travelling-salesman-based automated path searching (TAPS), we located the minimum-free-en"],"journal":["International journal of molecular sciences"],"pubmed_title":["Automated Path Searching Reveals the Mechanism of Hydrolysis Enhancement by T4 Lysozyme Mutants."],"pmcid":["PMC9736071"],"funding_grant_id":["31971179","JCYJ20200109150003938","HZQB-KCZYB-2020056","RCYX20200714114645019"],"pubmed_authors":["Xi K","Zhu L"],"additional_accession":[]},"is_claimable":false,"name":"Automated Path Searching Reveals the Mechanism of Hydrolysis Enhancement by T4 Lysozyme Mutants.","description":"Bacteriophage T4 lysozyme (T4L) is a glycosidase that is widely applied as a natural antimicrobial agent in the food industry. Due to its wide applications and small size, T4L has been regarded as a model system for understanding protein dynamics and for large-scale protein engineering. Through structural insights from the single conformation of T4L, a series of mutations (L99A,G113A,R119P) have been introduced, which have successfully raised the fractional population of its only hydrolysis-competent excited state to 96%. However, the actual impact of these substitutions on its dynamics remains unclear, largely due to the lack of highly efficient sampling algorithms. Here, using our recently developed travelling-salesman-based automated path searching (TAPS), we located the minimum-free-en","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2026-04-08T14:25:58.118Z","creation":"2025-04-04T23:37:09.431Z"},"accession":"S-EPMC9736071","cross_references":{"pubmed":["36498954"],"doi":["10.3390/ijms232314628"]}}