Mutant Proteins--Enzymes to Hydrolyze Toxic Organophosphates.
Abstract
This report discusses how the function of a protein is related to its three-dimensional structure and in turn to its sequence of amino acids, and how the various elements of a protein contribute to its structure stability. To gain the appropriated insights into the general rules that govern these relationships, we are developing and using various techniques of mutagenesis to alter the amino acid sequence in enzymes such as Beta-lactamase (responsible for resistance to penicillin therapy in many strains of infectious bacteria) and the serine protease alpha-lytic protease. We also employ novel chemical modifications of mutant proteins to achieve structures that cannot be obtained by purely biochemical approaches. The eventual objective is to be able to develop new enzymatic catalysts that, for example, will accelerate the hydrolysis of toxic organophosphates, some of which are potent nerve bases. Keywords: Antibiotic Resistance.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 15, 1987
- Accession Number
- ADA182210
Entities
People
- John H. Richards
Organizations
- California Institute of Technology