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In 1998, we published the data compilation PROTEIN STABILITY AND FOLDING which covered the data from the early beginnings of thermodynamic studies of protein folding until 1996. Since then, the amount of available thermodynamic data has increased nearly twice. The data constitute very important additions to the information on the protein folding problem, the construction of mutant protein, and the practical application of proteins in various fields. The Supplement covers the period 1997-1999 and is designed to make the vast amount of present data accessible to multidisciplinary research where chemistry, physics, biology, and medicine are involved and also biotechnology, pharmaceutical and food research. At the same time the data could be helpful to identify problems unsolved so far, and to avoid unnecessary duplication of scientific work. The structure of the Supplement is the same as in the previous data compilation. However, some additional data characterizing protein-denaturant interaction and protein unfolding by trifluoroethanol have been added. In that context, some previous data have been reconsidered. The author wishes to thank everyone who provided data, ideas, or even unpublished results. Furthermore, support by the Deutsche Forschungsgemeinschaft (INK 16 BI-I) is gratefully acknowledged. Finally, I would like to thank the staff of Springer Verlag for their efforts and for excellent assistance during the production of the data collections.
The modern biosciences make many new proteins available. Nevertheless the handling of these proteins is quite difficult due to problems with their stability. This updated and revised collection gives - in the form of tables - protein stability data for various temperatures and solvents.
The modern biosciences make many new proteins available. Nevertheless the handling of these proteins is quite difficult due to problems with their stability. This collection gives - in the form of tables - protein stability data for various temperatures and solvents. These data are most useful for the development of protein folding and the improvement of biotechnological stability for applications of proteins. The first supplement contains material covering 1997-1999. Some previous data have also been included into the present work. Previous papers on denaturant-induced protein unfolding have been reconsidered to include additional parameters. Furthermore, data on TFE-induced unfolding have been arranged in a new Table. Finally, some data have been added which slipped through during the preparation of the data collection.
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.
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.
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.
This collection of formulas has been written by applied scientists and industrial engineers for design professionals and students who work in engineering acoustics. It is subdivided into the most important fields of applied acoustics, each dealing with a well-defined type of problem. It provides easy and rapid access to profound and comprehensive information. In order to keep the text as concise as possible, the derivation of a formula is described only as far as necessary for its understanding. The interested reader can refer to the original source of the result. In addition to formulas, useful principles and computational procedures are given.
This volume includes 19 contributions to the 13th International Symposium on Analytical Ultracentrifugation which took place at the university of Osnabrück on March 6th and 7th, 2003. The contributions from leading scientists cover a broad spectrum of topics concerning: Technical Methods, Data Analysis, Innovations; Polymers, Colloids, Supramolecular Systems; Biological and Interaction Systems; Hydrodynamics and Modelling. Due to the increasing significance of Analytical Ultracentrifugation for both scientific and technical applications, this book will be an essential source of information with respect to recent developments and results related to this important analytical method.
This volume contains selected papers presented at the 42nd Biennial Meeting of the Kolloid-Gesellschaft held at the RWTH Aachen University September 26-28, 2005. The contributions in this volume represent the diversity of research topics in colloid and polymer science. They include the investigation of synthesis and properties of advanced temperature sensitive particles and their biomedical applications, drug delivery systems, foams, capsules, vesicles and gels, polyelectrolytes, nanoparticles surfactants and hybrid materials.
Protein interactions, which include interactions between proteins and other biomolecules, are essential to all aspects of biological processes, such as cell growth, differentiation, and apoptosis. Therefore, investigation and modulation of protein interactions are of significance as it not only reveals the mechanism governing cellular activity, but also leads to potential agents for the treatment of various diseases. The objective of this book is to highlight some of the latest approaches in the study of protein interactions, including modulation of protein interactions, development of analytical techniques, etc. Collectively they demonstrate the importance and the possibility for the further investigation and modulation of protein interactions as technology is evolving.