Biocatalyst design for stability and specificity
著者
書誌事項
Biocatalyst design for stability and specificity
（ACS symposium series, 516）
American Chemical Society, 1993
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注記
"Developed from a symposium sponsored by the Division of Biochemical Technology of the American Chemical Society at the Fourth Chemical Congress of North America (202nd National Meeting of the American Chemical Society), New York, New York, August 25-30, 1991"
Includes bibliographical references and indexes
内容説明・目次
内容説明
This title highlights the diversity of approaches used in understanding the function of proteins and how this understanding is applied to improving protein design for biotechnological applications. It reports on the status of current research into the interactions underlying protein stability, emphasizes the renaturation of functional properties from the aggregated state, and covers the relationship between protein structure and function, and the design of artificial multifunctional proteins by genetic technology. The book also reviews recent advances in the improvement of cellulase design through recombinant technology, and examines the use of chemical modification to improve enzymes.
目次
- Part 1 Protein stability: effects of mutations on thermodynamic properties or proteins, Julian M. Sturtevant
- contribution of hydrogen bonding and the hydrophobic effect to conformational stability of ribonuclease Tl, C. Nick Pace et al
- protein structure and stability assessment by circular dichroism spectroscopy, Mark C. Manning
- structure-function relationship of hyperthermophilic enzymes, Rainer Jaenicke
- psychrophilic proteinases from Atlantic cod, J.B. Bjarnason et al
- thermal and pH stress in thermal denaturation of trichoderman research cellobiohydrolase - supporting evidence for a two-transition model, John Baker and Michael E. Himmel
- recombinant protein stabilization through engineered metal-chelating sites, Pablo Umaiia et al
- engineering nonaqueous solvent-compatible enzymes, Frances H. Arnold et al. Protein folding: mutational effects on inclusion body formation, Ronald Wetzet and Boris A. Chrunyk
- characterization and refolding of b-lactamase inclusion bodies in escheria coli, Pascal Valax and George Georgiou
- participation of GroE heat shock proteins in polypeptide folding, Anthony A. Gatenby et al
- cosolvent effects on refolding and aggregation, Jeffrey L. Cleland and Daniel I.C. Wang
- facilitation of protein folding and the reversibility of denaturation, P.M. Horowitz. Part 3 Multifunctional proteins: artificial bifunctional enzymes - a tool to improve consecutive enzyme reactions and cell metabolism, Leif Bdlow
- proteins designed for adherence to cellulose, Edgar Ong et al
- modification of regulatory communication in aspartate transcarbamoylase, M.E. Wales et al
- C-tetrahydrofolate synthase - dissection of active site and domain structure by protein engineering, Anice E. Tbigpen et al. Part 4 Design of cellulases by recombinant methods: properties of native and site-mutagenized cellobiohydrolase, C. Barnett et al
- recombinant, beta-glucosidase of trichoderma reesei, Tim Fowler
- structure-function relationships in cellulase genes, David B. Wilson
- clostridium thermocellum cellulosome - new mechanistic concept for cellulose degradation, J.H. David Wu. Part 5 Improving natural enzymes by chemical cross-linking: protein chemical cross-linking - implications for protein stabilization, Shan S. Wong et al
- glutaraldehyde cross-linking - fast and slow modes, Timothy J.A. Johnson.
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