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- W2023208229 abstract "Numerous site-directed mutagenesis experiments have provided new insights into the stabilizing role of the individual forces and interactions within a globular protein molecule. Some useful guidelines and procedures are now available for producing genetically more stable proteins. Examples are the introduction of disulfide bonds, ion-binding sites, salt bridges, hydrophobic residues or hyrogen bonds, and the improvement of hydrophobic packing or α-helix propensity. Moreover, it is now clearly recognized that thermophilic (and, in general, extremophilic) bacteria produce highly stable proteins and enzymes of practical interest." @default.
- W2023208229 created "2016-06-24" @default.
- W2023208229 creator A5022652502 @default.
- W2023208229 date "1991-08-01" @default.
- W2023208229 modified "2023-09-24" @default.
- W2023208229 title "Analysis and modulation of protein stability" @default.
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- W2023208229 doi "https://doi.org/10.1016/0958-1669(91)90080-o" @default.
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