Protein Stability and Folding: Theory and Practice

ISBN-13: 9780896033016 / Angielski / Miękka / 1995 / 377 str.

Bret A. Shirley

Opis

The intent of this work is to bring together in a single volume the techniques that are most widely used in the study of protein stability and protein folding. Over the last decade our understanding of how p- teins fold and what makes the folded conformation stable has advanced rapidly. The development of recombinant DNA techniques has made possible the production of large quantities of virtually any protein, as well as the production of proteins with altered amino acid sequence. Improvements in instrumentation, and the development and refinement of new techniques for studying these recombinant proteins, has been central to the progress made in this field. To give the reader adequate background information about the s- ject, the first two chapters of this book review two different, yet related, aspects of protein stability. The first chapter presents a review of our current understanding of the forces involved in determining the conf- mational stability of proteins as well as their three-dimensional folds. The second chapter deals with the chemical stability of proteins and the pathways by which their covalent structure can degrade. The remainder of the book is devoted to techniques used in the study of these two major areas of protein stability, as well as several areas of active research. Although some techniques, such as X-ray crystallography and mass spectroscopy, are used in the study of protein stability, they are beyond the scope of this book and will not be covered extensively.

Recenzje

...very useful for any biochemist who needs to understand concepts of protein folding and stability and how protein folding can be monitored and studied. This is a good book for student researchers and should be considered as an addition to courses on protein structure.-Doody's Health Sciences Book Review Journal

Spis treści

Noncovalent Forces Important to the Conformational Stability of Protein Structures. Degradative Covalent Reactions Important to Protein Stability Fluorescence Spectroscopy. Ultraviolet Absorption Spectroscopy. Circular Dichroism. Infrared Spectroscopy. Identifying Sites of Posttranslational Modifications in Proteins via HPLC Peptide Mapping. Urea and Guanidine Hydrochloride Denaturation Curves. Differential Scanning Calorimetry. Disulfide Bonds in Protein Folding and Stability. Solvent Stabilization of Protein Structure. Site-Directed Mutagenesis to Study Protein Folding and Stability. Hydrogen Exchange Techniques. Protein Folding Kinetics. Molten Globules. Chaperonin-Assisted Protein Folding of the Enzyme Rhodanese by GroEL/GroES. Index.