Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/103599
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dc.contributor.authorAsial, Ignacioen
dc.contributor.authorCheng, Yue Xiangen
dc.contributor.authorEngman, Henriken
dc.contributor.authorDollhopf, Mariaen
dc.contributor.authorWu, Binghuangen
dc.contributor.authorNordlund, Pären
dc.contributor.authorCornvik, Tobiasen
dc.date.accessioned2014-05-15T02:35:35Zen
dc.date.accessioned2019-12-06T21:16:06Z-
dc.date.available2014-05-15T02:35:35Zen
dc.date.available2019-12-06T21:16:06Z-
dc.date.copyright2013en
dc.date.issued2013en
dc.identifier.citationAsial, I., Cheng, Y. X., Engman, H., Dollhopf, M., Wu, B., Nordlund, P., & Cornvik, T. (2013). Engineering protein thermostability using a generic activity-independent biophysical screen inside the cell. Nature Communications, 4.en
dc.identifier.issn2041-1723en
dc.identifier.urihttps://hdl.handle.net/10356/103599-
dc.description.abstractProtein stability is often a limiting factor in the development of commercial proteins and biopharmaceuticals, as well as for biochemical and structural studies. Unfortunately, identifying stabilizing mutations is not trivial since most are neutral or deleterious. Here we describe a high-throughput colony-based stability screen, which is a direct and biophysical read-out of intrinsic protein stability in contrast to traditional indirect activity-based methods. By combining the method with a random mutagenesis procedure, we successfully identify thermostable variants from 10 diverse and challenging proteins, including several biotechnologically important proteins such as a single-chain antibody, a commercial enzyme and an FDA-approved protein drug. We also show that thermostabilization of a protein drug using our approach translates into dramatic improvements in long-term stability. As the method is generic and activity independent, it can easily be applied to a wide range of proteins.en
dc.language.isoenen
dc.relation.ispartofseriesNature communicationsen
dc.rights© 2013 Macmillan Publishers Limited.en
dc.subjectDRNTU::Science::Biological sciencesen
dc.titleEngineering protein thermostability using a generic activity-independent biophysical screen inside the cellen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doi10.1038/ncomms3901en
dc.identifier.rims178830en
item.fulltextNo Fulltext-
item.grantfulltextnone-
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