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| Author | : Yoshiaki Nosoh |
| Publisher | : Ellis Horwood |
| Total Pages | : 234 |
| Release | : 1991 |
| Genre | : Science |
| ISBN | : |
| Author | : Ciarán ÓFágáin |
| Publisher | : Springer |
| Total Pages | : 224 |
| Release | : 1997-10-17 |
| Genre | : Medical |
| ISBN | : |
This book provides an account of our current knowledge of protein stability. It demonstrates how an understanding of protein stability has emerged from investigations of protein denaturation/inactivation and from studies on stabilizing interactions in proteins. It also describes the stability characteristics of enzymes in nonaqueous media and the special adaptations of thermophilic proteins. Manipulation of protein stability is outlined in chapters on the use of additives, chemical modification of proteins in solution, immobilization, protein engineering and long-term storage of proteins. The book includes numerous case studies and copious references to original research papers and relevant reviews and monographs.
| Author | : David S. Eisenberg |
| Publisher | : |
| Total Pages | : 334 |
| Release | : 1995 |
| Genre | : Science |
| ISBN | : 9780120342464 |
The topics covered by this volume include: protein destabilization at low temperatures; engineering the stability and function of Gene V Protein; free energy balance in protein folding; modelling protein stability as a heteropolymer collapse; stability of alpha helices; protein stability with T4 Lysozyme.
| Author | : Yoshiaki Nosoh |
| Publisher | : Ellis Horwood |
| Total Pages | : 234 |
| Release | : 1991 |
| Genre | : Science |
| ISBN | : |
| Author | : Anthony R. Rees |
| Publisher | : IRL Press |
| Total Pages | : 0 |
| Release | : 1992 |
| Genre | : Protein engineering |
| ISBN | : 9780199631384 |
Protein engineering is the rational modification or redesign of proteins using genetic engineering. Thus, it is now possible to modify enzyme specifics, remodel antibodies, and redesign many multi-domain proteins for therapeutic purposes. While the procedures for the introduction of mutations have become routine, predicting and understanding the effects of these mutations can be complicated. This volume provides a comprehensive guide to the methods used at every stage of the engineering process, from the choice of mutation strategy, through protein stability studies, to critical evaluations of mammalian, yeast, and bacterial host expression systems. Protein Engineering: A Practical Approach is the first practical guide to this fascinating mixture of molecular biology, protein structure analysis, computation, and biochemistry. It combines a thorough theoretical foundation with detailed protocols and will be invaluable to all research workers in the area, from graduate students to senior investigators.
| Author | : John F. Carpenter |
| Publisher | : Springer Science & Business Media |
| Total Pages | : 218 |
| Release | : 2012-12-06 |
| Genre | : Medical |
| ISBN | : 1461505577 |
Recombinant proteins and polypeptides continue to be the most important class of biotechnology-derived agents in today's pharmaceutical industry. Over the past few years, our fundamental understanding of how proteins degrade and how stabilizing agents work has made it possible to approach formulation of protein pharmaceuticals from a much more rational point of view. This book describes the current level of understanding of protein instability and the strategies for stabilizing proteins under a variety of stressful conditions.
| Author | : Ernst-Ludwig Winnacker |
| Publisher | : Springer Science & Business Media |
| Total Pages | : 141 |
| Release | : 2012-12-06 |
| Genre | : Science |
| ISBN | : 3642741738 |
Protein engineering has had considerable impact on basic and applied research in biochemistry and molecular biology. It is already in use as a tool in molecular biology, but it is beginning to strongly influence the planning of experiments in biology everywhere, and, with even fur ther-reaching consequences, the appointment politics in research in stitutions and industries. Protein engineering, perhaps more than any other methods of protein analysis and peptide synthesis, has shown that proteins are organic molecules governed by the universal laws of chemistry and physics. How ever, as was the case with other new powerful methods and techniques, protein engineering tempts to an exploration of its limitations and thus generates more questions than it answers. The 39th Mosbacher Colloquium on Protein Structure and Protein Engi neering is not the first conference on this topic and it will not be the last. The important issues are obviously techniques of protein en gineering, examples of application, and the basic framework of protein structure and stability within which reasonable experiments can be de signed; conversely also, what we can learn about protein structure, dynamics, and folding from such experiments. Experiments in this direc tion aim at elucidating the folding code in the long run, but help to exploit the role of individual amino acid residues in catalysis, pro tein stability, and binding specificity in selected proteins now.
| Author | : Peter Grunwald |
| Publisher | : World Scientific Publishing Company |
| Total Pages | : 1052 |
| Release | : 2009-03-02 |
| Genre | : Science |
| ISBN | : 1848168217 |
The book covers the fundamentals of the field of biocatalysis that are not treated in such detail (or even not at all) in existing biocatalysis books or biochemistry textbooks. It of course does not substitute existing biochemistry textbooks but will serve a suitable supplement as it discusses biochemical fundamentals in connection with the respective topics.With focus on the interdisciplinary nature of biocatalysis, the book contains many aspects of fundamental organic chemistry and some of inorganic chemistry as well, which should make it interesting not only for biochemistry but also for chemistry students. An important theme being emphasized in the book is that applied biocatalysis is one of the main prerequisites for a sustainable development.The topics covered ranges from basic enzyme chemistry (biosynthesis, structure, properties, interaction forces, kinetics) to a detailed description of catalytic mechanisms. It covers the fundamentals of the different enzyme classes together with their applications in native and in immobilized state or in the form of whole cells in aqueous as well as non-conventional media. Topics such as catalytic antibodies, nucleic acid catalysts, non-ribosomal peptide synthesis, evolutionary methods, and the design of cells are also included.
| Author | : Chau Q. Nguyen |
| Publisher | : |
| Total Pages | : 81 |
| Release | : 2010 |
| Genre | : |
| ISBN | : |
Abstract: Recent developments in the field of rational engineering have increased the awareness that surface residues and surface electrostatics of proteins are more important for protein stability than previously thought. In this study, we have analyzed the complicated sequence-stability-function relationship of the four helix-bundle protein Rop through combinatorial engineering of surface residues. Taking advantage of the function-structure relationship, we are able to screen a large library for functional variants with assumed native-like structure, based on a novel cell-based screen with GFP reporter. High-throughput thermal scanning (HTTS) and colony-based sequencing provide data to analyze the thermodynamic consequence of mutations. The data from 72 active variants reveal a number of interesting results. According to the expression screen, the four-helix bundle Rop displays some degree of tolerance to hydrophobic residues on its solvent-exposed region. Due to the simplicity of Rop's structure (entirely helix), charge neutralization and especially charge reversal substitutions do not seem to affect the protein stability. Moreover, it is encouraging to find a number of highly stabilized variants through rational and combinatorial engineering of surface residues. By using a four-helix bundle as a model protein, our results indicate great potential for stabilizing proteins with surface mutations; and the sites of stabilization can be selected so they do not interfere with protein function. Establishing a solid conclusion for the sequence-stability relationship of the surface mutants requires further ongoing work regarding high resolution structure analysis.
| Author | : Neha Arora |
| Publisher | : LAP Lambert Academic Publishing |
| Total Pages | : 56 |
| Release | : 2012 |
| Genre | : |
| ISBN | : 9783659193293 |
Chemical modification and protein engineering, by searching for homolog's in hyperthermophiles especially are useful tools for thermo stabilizing proteins, and also for elucidating the mechanism of protein stability that a single or a few amino acid replacement(s) in a protein is/are sufficient to enhance protein thermostability. Many eukaryotes have no homologs protein in the thermophilic organism; protein engineering would be necessary in such cases. Protein engineering may involve directed evolution. The factors affecting the thermal stability of proteins have been identified by comparison of the mesophilic and thermophilic protein belonging to the same protein family. Mainly it concern the tertiary structure of the proteins or their related proteins. One can replace amino acid(s) in a protein by mutagenesis. A promising strategy involves transfer of the identified gene into a thermophile and subsequent growth at higher temperatures. The thermodynamic thermal stability of a protein depends upon the differences in the enthalpy.
