Genetic engineering: Better enzymes by design
- 1 February 1985
- journal article
- Published by Springer Nature in Nature
- Vol. 313 (6004) , 630-631
- https://doi.org/10.1038/313630a0
Abstract
No abstract availableKeywords
This publication has 7 references indexed in Scilit:
- Amphiphilic Secondary Structure: Design of Peptide HormonesScience, 1984
- A large increase in enzyme–substrate affinity by protein engineeringNature, 1984
- Directed Mutagenesis of Dihydrofolate ReductaseScience, 1983
- Thiol-beta-lactamase: replacement of the active-site serine of RTEM beta-lactamase by a cysteine residue.Proceedings of the National Academy of Sciences, 1982
- Oligonucleotide-directed mutagenesis as a general and powerful method for studies of protein function.Proceedings of the National Academy of Sciences, 1982
- The conversion of serine at the active site of subtilisin to cysteine: a "chemical mutation".Proceedings of the National Academy of Sciences, 1966
- A New Enzyme Containing a Synthetically Formed Active Site. Thiol-Subtilisin1Journal of the American Chemical Society, 1966