Protein Structure, Stability, and Folding


Book Description

In Protein Structure, Stability, and Folding, Kenneth P. Murphy and a panel of internationally recognized investigators describe some of the newest experimental and theoretical methods for investigating these critical events and processes. Among the techniques discussed are the many methods for calculating many of protein stability and dynamics from knowledge of the structure, and for performing molecular dynamics simulations of protein unfolding. New experimental approaches presented include the use of co-solvents, novel applications of hydrogen exchange techniques, temperature-jump methods for looking at folding events, and new strategies for mutagenesis experiments. Unique in its powerful combination of theory and practice, Protein Structure, Stability, and Folding offers protein and biophysical chemists the means to gain a more comprehensive understanding of some of this complex area by detailing many of the major techniques in use today.




Protein Stability and Folding


Book Description

In Protein Stability and Folding: Theory and Practice, world-class scientists present in a single volume a comprehensive selection of hands-on recipes for all of the major techniques needed to understand the conformational stability of proteins, as well as their three-dimensional folding. The distinguished contributors provide clear, step-by-step instructions along with many troubleshooting tips, alternative procedures, and informative explanations about why certain steps are necessary. Even highly skilled researchers will find many time-saving methods. Among the techniques discussed are fluorescent, ultraviolet, and infrared spectroscopy; HPLC peptide mapping; differential scanning calorimetry; and hydrogen exchange. Shirley's Protein Stability and Folding: Theory and Practice will ensure a significant difference in the outcome of your experiments, producing the result desired even for beginners.




Rational Design of Stable Protein Formulations


Book Description

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.




Formulation, Characterization, and Stability of Protein Drugs


Book Description

Leading scientists offer detailed profiles of ten protein drugs currently in development. The case histories of these important new compounds are described from the perspective of their formulation, characterization, and stability. This ready reference also features recent data and an abundance of previously unpublished information. The in-depth coverage includes a highly useful compendium of degradation sites occurring in over 70 proteins. An invaluable aid in the rapid identification of potential `hot spots' in proteins, this accessible compilation allows for inspection of the protein's primary structure and preparation of a hydroflex plot.




Protein Stability


Book Description

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.







Protein Stability and Folding


Book Description

Protein folding remains one of the most exclusive problems of modern biochemistry. Structure analysis has given access to the wealth of the molecular architecture of pro teins. As architecture needs static calculations, protein structure is always related to thermodynamic factors that govern folding and stability of a particular folded protein over the non-organized polypeptide chain. During the past decades a huge amount of thermodynamic data related to protein folding and stability has been accumulated. The data are certainly of importance in dechiffring the protein folding problem. At the same time, the data can guide the con struction of modified and newly synthesized proteins with properties optimized for particular application. The intention of this book is a generation of a data collection which makes the vast amount of present data accessible for multidisciplinary research where chemistry, phy sics, biology, and medicine are involved and also pharmaceutical and food research and technology. It took several years to compile all the data and the author wishes to thank everyone who provided data, ideas or even unpublished results. The author is, in particular, indebted to Prof. Wadso (Lund, Sweden) and IUPAC's Steering Committee on Bio physical Chemistry. Furthermore, support by the Deutsche Forschungsgemeinschafi (INK 16 AI-I) is acknowledged.




Methods in Protein Structure and Stability Analysis: Conformational stability, size, shape, and surface of protein molecules


Book Description

Protein research is a frontier field in science. Proteins are widely distributed in plants and animals and are the principal constituents of the protoplasm of all cells, and consist essentially of combinations of a-amino acids in peptide linkages. Twenty different amino acids are commonly found in proteins, and serve as enzymes, structural elements, hormones, immunoglobulins, etc., and are involved throughout the body, and in photosynthesis. This book gathers new leading-edge research from throughout the world in this exciting and exploding field of research.




Thermostable Proteins


Book Description

This book covers the basic structural, thermodynamic and kinetic principles are covered and molecular strategies for the adaptation to high temperatures revealed by structure analysis are delineated. The roles of fluctuations, hydration and internal packing are thoroughly dicussed. Enzymes with a particular industrial importance, the subtilisin-like serine proteases, have been extensively studied by protein engineering. One extensive chapter is devoted to the present state of knowledge concerning structure-function relations and the origin of the their structural stability. Last but not least, computational and experimental approaches for the design of proteins with increased thermal stability based on sequences or 3D structures are present




Protein Bioinformatics


Book Description

One of the most pressing tasks in biotechnology today is to unlock the function of each of the thousands of new genes identified every day. Scientists do this by analyzing and interpreting proteins, which are considered the task force of a gene. This single source reference covers all aspects of proteins, explaining fundamentals, synthesizing the latest literature, and demonstrating the most important bioinformatics tools available today for protein analysis, interpretation and prediction. Students and researchers of biotechnology, bioinformatics, proteomics, protein engineering, biophysics, computational biology, molecular modeling, and drug design will find this a ready reference for staying current and productive in this fast evolving interdisciplinary field. - Explains all aspects of proteins including sequence and structure analysis, prediction of protein structures, protein folding, protein stability, and protein interactions - Presents a cohesive and accessible overview of the field, using illustrations to explain key concepts and detailed exercises for students.