Download or read book The Protein Folding Problem and Its Solutions written by Arieh Ben-Naim and published by World Scientific Publishing Company Incorporated. This book was released on 2013 with total page 297 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Download or read book The Protein Folding Problem and Tertiary Structure Prediction written by Kenneth M.Jr. Merz and published by Springer Science & Business Media. This book was released on 2012-12-06 with total page 585 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Download or read book Molecular Biology of the Cell written by and published by . This book was released on 2002 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book NMR in Structural Biology written by Kurt Wthrich and published by World Scientific. This book was released on 1995 with total page 770 pages. Available in PDF, EPUB and Kindle. Book excerpt: The volume presents a survey of the research by Kurt Wthrich 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.
Download or read book Protein Physics written by Alexei V. Finkelstein and published by Elsevier. This book was released on 2016-06-22 with total page 530 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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
Download or read book Protein Stability and Folding written by Wolfgang Pfeil and published by Springer Science & Business Media. This book was released on 2012-12-06 with total page 662 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Download or read book Protein Folding in Silico written by Irena Roterman-Konieczna and published by Elsevier. This book was released on 2012-10-04 with total page 241 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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
Download or read book Proteins written by David Whitford and published by John Wiley & Sons. This book was released on 2013-04-25 with total page 544 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Download or read book The Protein Folding Problem written by Donald B Wetlaufer and published by Routledge. This book was released on 2019-06-21 with total page 161 pages. Available in PDF, EPUB and Kindle. Book excerpt: Proteins in living systems carry out a great variety of specific functions, each of which depends on the precise three-dimensional structure of a particular protein. Proteins are synthesized in the form of a flexible polypeptide chain that is capable of assuming a vast number of configurations; the transformation of this chain into a specific, relatively rigid three-dimensional structure is called folding--a remarkable process of self-organization. It is known that the amino acid sequences of some proteins have sufficient information to determine their three-dimensional structures. There are other proteins whose folding requires additional information beyond that found in the sequence of the mature protein. This book introduces the central problem of folding mechanisms as well as a number of other closely related issues. This book is neither a textbook nor a treatise. Rather, it is an attempt by several investigators to convey the excitement and challenges of those aspects of the folding problem in which they are actively engaged. The contributors give brief introductions to protein folding from the perspectives of molecular architecture, stability and dynamics, phage genetics, DNA exons, general physiology, and natural selection. They point out emerging new directions, including the suggestion of a class of diseases that result from protein folding defects.
Download or read book Protein Folding written by Alka Dwevedi and published by Springer. This book was released on 2014-12-01 with total page 61 pages. Available in PDF, EPUB and Kindle. Book excerpt: The book will discuss classes of proteins and their folding, as well as the involvement of bioinformatics in solving the protein folding problem. In vivo and in vitro folding mechanisms are examined, as well as the failures of in vitro folding, a mechanism helpful in understanding disease caused by misfolding. The role of energy landscapes is also discussed and the computational approaches to these landscapes.
Download or read book Protein Folding Misfolding and Aggregation written by Victor Muñoz and published by Royal Society of Chemistry. This book was released on 2008 with total page 290 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Download or read book Oxidative Folding of Peptides and Proteins written by Luis Moroder and published by Royal Society of Chemistry. This book was released on 2009 with total page 453 pages. Available in PDF, EPUB and Kindle. Book excerpt: With contributions from experts in the field, this book provides a comprehensive overview of the oxidative folding of cysteine-rich peptides.
Download or read book Fundamentals of Protein Structure and Function written by Engelbert Buxbaum and published by Springer. This book was released on 2015-11-27 with total page 521 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book serves as an introduction to protein structure and function. Starting with their makeup from simple building blocks, called amino acids, the 3-dimensional structure of proteins is explained. This leads to a discussion how misfolding of proteins causes diseases like cancer, various encephalopathies, or diabetes. Enzymology and modern concepts of enzyme kinetics are then introduced, taking into account the physiological, pharmacological and medical significance of this often neglected topic. This is followed by thorough coverage of hæmoglobin and myoglobin, immunoproteins, motor proteins and movement, cell-cell interactions, molecular chaperones and chaperonins, transport of proteins to various cell compartments and solute transport across biological membranes. Proteins in the laboratory are also covered, including a detailed description of the purification and determination of proteins, as well as their characterisation for size and shape, structure and molecular interactions. The book emphasises the link between protein structure, physiological function and medical significance. This book can be used for graduate and advanced undergraduate classes covering protein structure and function and as an introductory text for researchers in protein biochemistry, molecular and cell biology, chemistry, biophysics, biomedicine and related courses. About the author: Dr. Buxbaum is a biochemist with interest in enzymology and protein science. He has been working on the biochemistry of membrane transport proteins for nearly thirty years and has taught courses in biochemistry and biomedicine at several universities.
Download or read book Mechanisms of Protein Folding written by Roger H. Pain and published by Oxford University Press, USA. This book was released on 2000 with total page 433 pages. Available in PDF, EPUB and Kindle. Book excerpt: Since the publication of the first edition of mechanisms of protein folding in 1994, significant advances in both the technical and conceptual understanding of protein folding. This new edition has been brought up to date in content, context, and authorship and will make the subject accessibleto a wide range of scientists. The emphasis on experimental approaches has benn maintained from the first edition but this time within the explicit context of simulations and energy surfaces. There is an introductory chapter explaining the 'new' model of protein folding, which takes into account theheterogeneity of the starting state. Advances in interpreting observed kinetic data and the development of technology to observe fast folding reactions and characterize intermediate structures have accompanied this new view and are covered in detail. The term 'molten globule'is often usedincorrectly but here the significance of the term is carefully described at different satges of folding. The concept of the transition state, including the complementary approaches of molecular dynamics and protein engineering, is also discussed in detail. In vitro studies provide the molecularbasis for the thermodynamic and kinetic energy minimization of the in vivo processes of protein folding and two of the potentially rate determining reactions are disulphide bond formation and proline isomerization. It has also become increasingly apparent that chaperone proteins play a vital role inprotein folding and other reactions of proteins involoving major conformational change and the molecular details of these processes are discussed in detail in chapter 14. The final chapter describes the centreal importance of protein folding and unfolding reactions in disease and gives claerdefinition of the term 'misfolding'. Studying protein folding in vivo is full of problems and to show how these problems can be overcome in practice, three case studies of three very different types of protein have been included: the small globular protein apomyoglobin; the fibrous protein collagen;and the membrane protein haemagglutinin.
Download or read book Handbook on Biological Networks written by Stefano Boccaletti and published by World Scientific. This book was released on 2010 with total page 465 pages. Available in PDF, EPUB and Kindle. Book excerpt: Networked systems are all around us. The accumulated evidence of systems as complex as a cell cannot be fully understood by studying only their isolated constituents, giving rise to a new area of interest in research OCo the study of complex networks . In a broad sense, biological networks have been one of the most studied networks, and the field has benefited from many important contributions. By understanding and modeling the structure of a biological network, a better perception of its dynamical and functional behavior is to be expected. This unique book compiles the most relevant results and novel insights provided by network theory in the biological sciences, ranging from the structure and dynamics of the brain to cellular and protein networks and to population-level biology. Sample Chapter(s). Chapter 1: Introduction (61 KB). Contents: Networks at the Cellular Level: The Structural Network Properties of Biological Systems (M Brilli & P Li); Dynamics of Multicellular Synthetic Gene Networks (E Ullner et al.); Boolean Networks in Inference and Dynamic Modeling of Biological Systems at the Molecular and Physiological Level (J Thakar & R Albert); Complexity of Boolean Dynamics in Simple Models of Signaling Networks and in Real Genetic Networks (A D az-Guilera & R ulvarez-Buylla); Geometry and Topology of Folding Landscapes (L Bongini & L Casetti); Elastic Network Models for Biomolecular Dynamics: Theory and Application to Membrane Proteins and Viruses (T R Lezon et al.); Metabolic Networks (M C Palumbo et al.); Brain Networks: The Human Brain Network (O Sporns); Brain Network Analysis from High-Resolution EEG Signals (F De Vico Fallani & F Babiloni); An Optimization Approach to the Structure of the Neuronal layout of C elegans (A Arenas et al.); Cultured Neuronal Networks Express Complex Patterns of Activity and Morphological Memory (N Raichman et al.); Synchrony and Precise Timing in Complex Neural Networks (R-M Memmesheimer & M Timme); Networks at the Individual and Population Levels: Ideas for Moving Beyond Structure to Dynamics of Ecological Networks (D B Stouffer et al.); Evolutionary Models for Simple Biosystems (F Bagnoli); Evolution of Cooperation in Adaptive Social Networks (S Van Segbroeck et al.); From Animal Collectives and Complex Networks to Decentralized Motion Control Strategies (A Buscarino et al.); Interplay of Network State and Topology in Epidemic Dynamics (T Gross). Readership: Advanced undergraduates, graduate students and researchers interested in the study of complex networks in a wide range of biological processes and systems."
Download or read book The State of Science written by Marc Zimmer and published by Rowman & Littlefield. This book was released on 2020-07-20 with total page 221 pages. Available in PDF, EPUB and Kindle. Book excerpt: New research and innovations in the field of science are leading to life-changing and world-altering discoveries like never before. What does the horizon of science look like? Who are the scientists that are making it happen? And, how are we to introduce these revolutions to a society in which a segment of the population has become more and more skeptical of science? Climate change is the biggest challenge facing our nation, and scientists are working on renewable energy sources, meat alternatives, and carbon dioxide sequestration. At the same time, climate change deniers and the politicization of funding threaten their work. CRISPR, (Clustered Regularly Interspaced Short Palindromic Repeats) repurposes bacterial defense systems to edit genes, which can change the way we live, but also presents real ethical problems. Optogenetics will help neuroscientists map complicated neural circuitry deep inside the brain, shedding light on treating Alzheimer’s and Parkinson’s disease. Zimmer also investigates phony science ranging from questionable “health” products to the fervent anti-vaccination movement. Zimmer introduces readers to the real people making these breakthroughs. Concluding with chapters on the rise of women in STEM fields, the importance of US immigration policies to science, and new, unorthodox ways of DIY science and crowdsource funding, The State of Science shows where science is, where it is heading, and the scientists who are at the forefront of progress.
Download or read book Solvent Induced Interactions and Forces in Protein Folding written by Arieh Ben-Naim and published by Springer Nature. This book was released on 2023-06-12 with total page 185 pages. Available in PDF, EPUB and Kindle. Book excerpt: This monograph presents the molecular theory and necessary tools for the study of solvent-induced interactions and forces. After introducing the reader to the basic definitions of solvent-induced interactions, the author provides a brief analysis of the statistical thermodynamics. The book thoroughly overviews the connection of those interactions with thermodynamics and consequently focuses on specifically discussing the hydrophobic-hydrophilic interactions and forces. The importance of the implementation of hydrophilic interactions and forces in various biochemical processes is thoroughly analyzed, while evidence based on theory, experiments, and simulated calculations supporting that hydrophilic interactions and forces are far more important than the corresponding hydrophobic effects in many biochemical processes such as protein folding, self-assembly of proteins, molecular recognitions, are described in detail. This title is of great interest to students and researchers working in the fields of chemistry, physics, biochemistry, and molecular biology.
