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dc.contributor.authorKollman, P.
dc.date.accessioned2023-11-03T09:17:17Z
dc.date.available2023-11-03T09:17:17Z
dc.date.issued1989
dc.date.submitted2023-11-03
dc.identifier.citationAdvances in protein design, 57 - 64en_US
dc.identifier.isbn3527280243
dc.identifier.isbn0895739534
dc.identifier.issn0930-4320
dc.identifier.urihttp://hdl.handle.net/10033/623520
dc.description.abstractWegive a brief review ofthe theoretical methodology andfree energy perturbation applications to proteins. We show that theoretical methods are capable of complementing experimental studies in leading to a clearer understanding ofthe effect of site specific mutations onligand binding, enzymecatalysis and protein stability.en_US
dc.language.isoenen_US
dc.publisherGBF Gesellschaft für Biotechnologische Forschung mbH, Braunschweigen_US
dc.relation.ispartofseriesGBF monographs ; Volume 12en_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleComputer Simulations Applied to Site Specific Mutagenesis and Ligand Binding: The Use of Free Energy Perturbation Methodsen_US
dc.typeBook chapteren_US
dc.typeconference paperen_US
dc.contributor.departmentDepartment of Pharmaceutical Chemistry University of California, San Franciscoen_US
dc.identifier.journalAdvances in protein design, 1988en_US
refterms.dateFOA2023-11-03T09:17:18Z


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