Engineering Enzyme Stability and Resistance to an Organic Cosolvent by Modification of Residues in the Access Tunnel

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F13%3A00066682" target="_blank" >RIV/00216224:14310/13:00066682 - isvavai.cz</a>
Alternative codes found
RIV/67179843:_____/13:00425304 RIV/68378050:_____/13:00425304 RIV/60076658:12310/13:43885238 RIV/60076658:12520/13:43885238
Result on the web
<a href="http://dx.doi.org/10.1002/anie.201206708" target="_blank" >http://dx.doi.org/10.1002/anie.201206708</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/anie.201206708" target="_blank" >10.1002/anie.201206708</a>

Result language
angličtina
Original language name
Engineering Enzyme Stability and Resistance to an Organic Cosolvent by Modification of Residues in the Access Tunnel
Original language description
Mutations targeting as few as four residues lining the access tunnel extended enzyme?s half-life in 40% dimethyl sulfoxide from minutes to weeks (4,000-fold) and increased its melting temperature by 19 Grades C. Protein crystallography and molecular dynamics revealed that the tunnel residue packing is a key determinant of protein stability and the active-site accessibility for co-solvent molecules (red dots). The broad applicability of this concept was verified by analyzing twenty six proteins with buried active sites from all six enzyme classes.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
—

Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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