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dc.contributor.authorVerma, Rajni
dc.contributor.authorWong, Tuck Seng
dc.contributor.authorSchwaneberg, Ulrich
dc.contributor.authorRoccatano, Danilo
dc.identifier.citationVerma, Rajni; Wong, Tuck Seng; Schwaneberg, Ulrich; Roccatano, Danilo. 2014. Chapter 19 -- The Mutagenesis Assistant Program. In: Directed Evolution Library Creation, Methods in Molecular Biology, vol. 1179:pp 279-290en_US
dc.descriptionClick on the DOI link to access the article (may not be free).en_US
dc.description.abstractMutagenesis Assistant Program (MAP) is a web-based statistical tool to develop directed evolution strategies by investigating the consequences at the amino acid level of the mutational biases of random mutagenesis methods on any given gene. The latest development of the program, the MAP(2.0)3D server, correlates the generated amino acid substitution patterns of a specific random mutagenesis method to the sequence and structural information of the target protein. The combined information can be used to select an experimental strategy that improves the chances of obtaining functionally efficient and/or stable enzyme variants. Hence, the MAP(2.0)3D server facilitates the "in silico" prescreening of the target gene by predicting the amino acid diversity generated in a random mutagenesis library. Here, we describe the features of MAP(2.0)3D server by analyzing, as an example, the cytochrome P450(BM3) monooxygenase (CYP102A1). The MAP(2.0)3D server is available publicly at
dc.publisherSpringer International Publishing AGen_US
dc.relation.ispartofseriesDirected Evolution Library Creation, Methods in Molecular Biology;v.1179
dc.subjectDirected evolutionen_US
dc.subjectRandom mutagenesis methodsen_US
dc.subjectMutational biasen_US
dc.subjectResidue mutability indicatoren_US
dc.subjectProtein engineeringen_US
dc.titleChapter 19 -- The Mutagenesis Assistant Programen_US
dc.typeBook chapteren_US
dc.rights.holderCopyright © 2014, Springer Science+Business Media New York
dc.rights.holder© Springer International Publishing AG, Part of Springer Science+Business Media

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