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• W2155758860 abstract "Mutations targeting as few as four residues lining the access tunnel extended the half-life of an enzyme in 40 % dimethyl sulfoxide from minutes to weeks and increased its melting temperature by 19 °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 cosolvent molecules (red dots)." @default.
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• W2155758860 date "2013-01-09" @default.
• W2155758860 modified "2023-10-18" @default.
• W2155758860 title "Engineering Enzyme Stability and Resistance to an Organic Cosolvent by Modification of Residues in the Access Tunnel" @default.
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• W2155758860 doi "https://doi.org/10.1002/anie.201206708" @default.
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