The Protein Folding Problem and Its Solutions PDF Download

Author: Arieh Ben-Naim
Publisher: World Scientific Publishing Company Incorporated
ISBN: 9789814436359
Category : Science
Languages : en
Pages : 297

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Book Description
This book presents a new approach to the Protein Folding Problem. It starts with a clear description of what the protein folding problem involves. Then, it suggests non-conventional answers to some of the questions posed. In particular, it emphasizes the importance of hydrophilic interactions and hydrophilic forces, rather than the hydrophobic effects, for the stability of the native structure of proteins, as well for the speed of the folding process.

Author: Kenneth M.Jr. Merz
Publisher: Springer Science & Business Media
ISBN: 1468468316
Category : Science
Languages : en
Pages : 585

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Book Description
A solution to the protein folding problem has eluded researchers for more than 30 years. The stakes are high. Such a solution will make 40,000 more tertiary structures available for immediate study by translating the DNA sequence information in the sequence databases into three-dimensional protein structures. This translation will be indispensable for the analy sis of results from the Human Genome Project, de novo protein design, and many other areas of biotechnological research. Finally, an in-depth study of the rules of protein folding should provide vital clues to the protein fold ing process. The search for these rules is therefore an important objective for theoretical molecular biology. Both experimental and theoretical ap proaches have been used in the search for a solution, with many promising results but no general solution. In recent years, there has been an exponen tial increase in the power of computers. This has triggered an incredible outburst of theoretical approaches to solving the protein folding problem ranging from molecular dynamics-based studies of proteins in solution to the actual prediction of protein structures from first principles. This volume attempts to present a concise overview of these advances. Adrian Roitberg and Ron Elber describe the locally enhanced sam pling/simulated annealing conformational search algorithm (Chapter 1), which is potentially useful for the rapid conformational search of larger molecular systems.

Author: Wolfgang Pfeil
Publisher: Springer Science & Business Media
ISBN: 3642587607
Category : Science
Languages : en
Pages : 662

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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.

Author: Alexei V. Finkelstein
Publisher: Elsevier
ISBN: 0081012365
Category : Science
Languages : en
Pages : 530

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Book Description
Protein Physics: A Course of Lectures covers the most general problems of protein structure, folding and function. It describes key experimental facts and introduces concepts and theories, dealing with fibrous, membrane, and water-soluble globular proteins, in both their native and denatured states. The book systematically summarizes and presents the results of several decades of worldwide fundamental research on protein physics, structure, and folding, describing many physical models that help readers make estimates and predictions of physical processes that occur in proteins. New to this revised edition is the inclusion of novel information on amyloid aggregation, natively disordered proteins, protein folding in vivo, protein motors, misfolding, chameleon proteins, advances in protein engineering & design, and advances in the modeling of protein folding. Further, the book provides problems with solutions, many new and updated references, and physical and mathematical appendices. In addition, new figures (including stereo drawings, with a special appendix showing how to use them) are added, making this an ideal resource for graduate and advanced undergraduate students and researchers in academia in the fields of biophysics, physics, biochemistry, biologists, biotechnology, and chemistry. - Fully revised and expanded new edition based on the latest research developments in protein physics - Written by the world's top expert in the field - Deals with fibrous, membrane, and water-soluble globular proteins, in both their native and denatured states - Summarizes, in a systematic form, the results of several decades of worldwide fundamental research on protein physics and their structure and folding - Examines experimental data on protein structure in the post-genome era

Author: Kurt Wthrich
Publisher: World Scientific
ISBN: 9789810223847
Category : Science
Languages : en
Pages : 770

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Book Description
The volume presents a survey of the research by Kurt Wthrich and his associates during the period 1965 to 1994. A selection of reprints of original papers on the use of NMR spectroscopy in structural biology is supplemented with an introduction, which outlines the foundations and the historical development of the use of NMR spectroscopy for the determination of three-dimensional structures of biological macromolecules in solution. The original papers are presented in groups highlighting protein structure determination by NMR, studies of dynamic properties and hydration of biological macromolecules, and practical applications of the NMR methodology in fields such as enzymology, transcriptional regulation, immunosuppression and protein folding.

Author:
Publisher:
ISBN: 9780815332183
Category : Cells
Languages : en
Pages : 0

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Book Description

Author: Luis Moroder
Publisher: Royal Society of Chemistry
ISBN: 0854041486
Category : Science
Languages : en
Pages : 453

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Book Description
With contributions from experts in the field, this book provides a comprehensive overview of the oxidative folding of cysteine-rich peptides.

Author: Irena Roterman-Konieczna
Publisher: Elsevier
ISBN: 1908818255
Category : Science
Languages : en
Pages : 241

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Book Description
Protein folding is a process by which a protein structure assumes its functional shape of conformation, and has been the subject of research since the publication of the first software tool for protein structure prediction. Protein folding in silico approaches this issue by introducing an ab initio model that attempts to simulate as far as possible the folding process as it takes place in vivo, and attempts to construct a mechanistic model on the basis of the predictions made. The opening chapters discuss the early stage intermediate and late stage intermediate models, followed by a discussion of structural information that affects the interpretation of the folding process. The second half of the book covers a variety of topics including ligand binding site recognition, the "fuzzy oil drop" model and its use in simulation of the polypeptide chain, and misfolded proteins. The book ends with an overview of a number of other ab initio methods for protein structure predictions and some concluding remarks. - Discusses a range of ab initio models for protein structure prediction - Introduces a unique model based on experimental observations - Describes various methods for the quantitative assessment of the presented models from the viewpoint of information theory

Author: David Whitford
Publisher: John Wiley & Sons
ISBN: 1118685725
Category : Science
Languages : en
Pages : 544

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Book Description
Proteins: Structure and Function is a comprehensive introduction to the study of proteins and their importance to modern biochemistry. Each chapter addresses the structure and function of proteins with a definitive theme designed to enhance student understanding. Opening with a brief historical overview of the subject the book moves on to discuss the ‘building blocks’ of proteins and their respective chemical and physical properties. Later chapters explore experimental and computational methods of comparing proteins, methods of protein purification and protein folding and stability. The latest developments in the field are included and key concepts introduced in a user-friendly way to ensure that students are able to grasp the essentials before moving on to more advanced study and analysis of proteins. An invaluable resource for students of Biochemistry, Molecular Biology, Medicine and Chemistry providing a modern approach to the subject of Proteins.

Author: Victor Muñoz
Publisher: Royal Society of Chemistry
ISBN: 0854042571
Category : Science
Languages : en
Pages : 290

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Book Description
Protein folding and aggregation is the process by which newly synthesized proteins fold into the specific three-dimensional structures defining their biologically active states. It has always been a major focus of research in biochemistry and has often been seen as the unsolved second part of the genetic code. In the last 10 years we have witnessed a quantum leap in the research in this exciting area. Computational methods have improved to the extent of making possible to simulate the complete folding process of small proteins and the early stages of protein aggregation. Experimental methods h.