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Protein Folding Handbook 5-volume set
Manufacturer: Wiley-VCH
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Binding: Hardcover
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ASIN: 3527307842 |
Book Description
This unique handbook contains the expertise from more than 60 research groups, covering the entire range of topics in protein folding - from biophysics to molecular medicine.
The first part explains the principles and factors governing protein stability, and how this knowledge may be used to predict folding pathways. It also surveys important techniques used to study the protein folding process, including spectroscopic, chemical and biological techniques.
The second part is devoted to protein folding, unfolding, and misfolding in the cellular context, introducing chaperones and other enzymes involved in protein folding, as well as a study of the pathophysiology of misfolded proteins in amyloid and other disease states. The whole is rounded off by a discussion of the possibility of interfering with the protein folding process by genetic engineering.
The comprehensiveness and outstanding quality of the carefully selected contents make this the ultimate reference for every scientist with an interest in protein folding.
Average customer rating:
- A lot of information, but not-so-well explained...
- Highly recommend it
- essential
- Biochemists Can't Miss
- The Mother of All Enzyme Books
|
Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding
Alan Fersht
Manufacturer: W. H. Freeman
ProductGroup: Book
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Similar Items:
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Protein Stucture and Function (Primers in Biology)
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Proteins: Structures and Molecular Properties
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Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Wiley Classics Library)
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Enzymes: A Practical Introduction to Structure, Mechanism, and Data Analysis
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Introduction to Protein Structure: Second Edition
ASIN: 0716732688 |
Customer Reviews:
A lot of information, but not-so-well explained..........2005-04-13
With an undergrad degree in chemistry and a year of graduate school (granted, without a focus solely in biochemistry), this text was often difficult for me to follow and gain much from. Though the text contained an impressive breadth of topics, this breadth came at the cost of depth. In my opinion, a textbook should more-or-less stand on its own in providing a clear understanding of a topic. All too often I didn't find this to be the case with the Fersht book. Instead, I often had to consult many of the references listed in the text to obtain sufficient understanding of topics. (Fortunately, the book includes extensive reference lists.) If looking up endless references (many old and sometimes difficult to obtain) is something you enjoy, this book is for you.--If not, forget it!
Highly recommend it.......2003-08-31
Hands down the bible of enzyme kinetics!
Anyone looking to learn more about enzyme kinetics, thermodynamics, structure, and function will find this book clear, thoughtfully written, and at the forefront in the field.
essential.......2002-05-01
If you are studying protein structure, you probably should read this book for reference.
This is solely my opinion, but I have learned new things and reinforced some old knowledge, as well. The book is well-written, and understandable, without being simplistic.
Some texts are difficult to understand, or dry, or facile. This is not one of those texts.
Biochemists Can't Miss.......2001-08-23
The book focuses on enzyme catalysis, stereochemistry of enzyme reactions, determination of rate constant, enzyme kinetics, and protein structure and folding. It would be an ideal reference for the study of protein chemistry. It can serve as the primary text for an advanced course in protein chemistry or a supplement for undergraduate biochemistry text.
Protein folding has remained one of the most intricate yet less understood process in modern biochemistry. Feersht's treatise of the subject in this book is splendid. The author overviews protein structure and diversity in the opening chapter. What I find really precious about this book is the discussion on protein engineering, forces on folding, and recombinant DNA technology in the context of protein folding.
Aside from protein chemistry, the chapter on chemical catalysis is excellent in learning more about transition state theory, general acid/base catalysis, covalent catalysis, structure-reactivity relationships, and kinetic isotope effects.
The Mother of All Enzyme Books.......2001-01-10
Man, this book rocked! I took one look at the ribbon structure of ATPase on the cover and said to myself, "Whoa dude! This is, like, phat!" Then I turned the pages and BAM! I was knee deep in protein structure! Like, any first-year biochemist knows its all about the acids, as in amino, and Fersht, he knows his peptides! Oh man, I was on cloud nine! And I've been off my meds for two months now! But you wanna know the real dope? You can't say diddly about function unless you know structure, and that Alan, as in Fersht, dude! Like, he starts you off simple, like, you know, with the "building blocks," like we're a bunch of two-year-olds, and you string 'em together and get all that higher-order structure and stuff, and slowly, ever so slowly, like a mental itch that invades your consciousness and becomes screaming voices telling you to AHHHHHHHHH! So many domains! Too many functional units! No, no, nooooooo! Schiff base? Shift Bass! Ah HA HA HA HA! What do all those K's mean!?! Take me home! Please...
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Mechanisms of Protein Folding
Manufacturer: Oxford University Press, USA
ProductGroup: Book
Binding: Paperback
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ASIN: 0199637881 |
Book Description
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 accessible to 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 the heterogeneity 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 used incorrectly 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 molecular basis 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 in protein 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 claer definition 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.
Book Description
Why do women stabilize our societies? Why can we enjoy and understand Shakespeare? Why are fruitflies uniform? Why do omnivorous eating habits aid our survival? Why is Mona Lisa’s smile beautiful? – Is there any answer to these questions? This book shows that the statement: "weak links stabilize complex systems" holds the answers to all of the surprising questions above. The author (recipient of several distinguished science communication prizes) uses weak (low affinity, low probability) interactions as a thread to introduce a vast variety of networks from proteins to ecosystems. Many people, from Nobel Laureates to high-school students have helped to make the book understandable to all interested readers. This unique book and the ideas it develops will have a significant impact on many, seemingly diverse, fields of study.
Customer Reviews:
Primer on real-life networks with a theme .......2007-02-02
If you ever needed another good reason to value your grandmother even more, you'll find the answer in "Weak links".
Structurally, his book starts with an exposition on network theory and
terminology, then the application and discussion of these concepts to
real-life complex systems on many scales and applied to many domains (physical, natural, technological, social). His main point is, as the reviewer noted above, that 'weak' links (weak: additional/removal does not statistically affect the average of some metric) stabilize systems.
The book has thorough footnotes, one can delve as deep as one would like
into the professional papers. In addition, Csermely is an honest scholar - he shows his hands when there is mere speculation (you have to see the book's unique pictograms to appreciate the effects)
After pouring through several alternatives, I have adopted this book as a
textbook for my Science of Networks class (I'm CS fac at an elite US liberal arts school), and I recommend it to anyone without hesitation for a readable, and learned exposition.
I only have two or three caveats from a specialist's point of view: The
phenomenological discovery of power laws in complex systems is not unusual
and may not be evidence of any SF properties. Scale-free is an abused
term, and I wish the controversy about it were explained a bit more. Also, from a modelling point of view, I wish Doyle and Carlson's work on HOT systems were discussed in more depth.
But these are minor points, relatively speaking. This is a gem of a book:
erudite, humane, funny, accessible and thoroughly fascinating. On every
page, there are delights that lead down new intellectual paths.
Csermely did a great service to pedagogy and to this budding science with
this magisterial survey. Outstanding in its ease of access for intelligent
undergraduates and commendable for intellectual honesty - I wish more
books (textbooks and otherwise) were written this way.
Weak Links Stabilize Complex Systems.......2006-05-13
It is an intriguing concept.
Weak links, invisible in many networks, are critical to its stability. In this book, Peter Csermely shows that all networks, from the universe to molecules are governed by the same principles. Regardless of the system -- atoms, cells, companies, web pages or countries -- surprisingly, the weak links stabilize each.
Csermely, a professor at Semmelweis University in Budapest, a former Fogarty Fellow at Harvard University, is a molecular chaperones specialist. In 2003, he became fascinated by the concept of affinity -- a network's stabilizing components of must have weak links to the other components. These weak links act as hubs. Attack the hubs; disrupt the network.
Csermely demonstrates the concept hold true in field after field. The professor begins his study with a discussion of the Granovetter study of a job search and then proceeds to describe network dynamics. By chapter four, the reader is ready to be introduced to the concept of weak links as universal stabilizers. Then, the professor conducts a network tour ranging from macromolecules to the planet earth. Finally he ends with a discussion of weak links, stability landscapes and game theory.
Surprisingly, his book is understandable, even to non-academics. It is loaded with gems that can be applied to the reader's networks and relationships.
This is not a book I would have ever picked up on my own. Thankfully, Professor Csermely sent me an advanced copy. It is a unique book that takes a thorough look at an intriguing concept.
Book Description
This book introduces an approach to protein folding from the point of view of kinetic theory. There is an abundance of data on protein folding, but few proposals are available on the mechanism driving the process. Here, presented for the first time, are suggestions on possible research directions, as developed by the author in collaboration with C C Lin.
The first half of this invaluable book contains a concise but relatively complete review of relevant topics in statistical mechanics and kinetic theory. It includes standard topics such as thermodynamics, the Maxwell-Boltzmann distribution, and ensemble theory. Special discussions include the dynamics of phase transitions, and Brownian motion as an illustration of stochastic processes.
The second half develops topics in molecular biology and protein structure, with a view to discovering mechanisms underlying protein folding. Attention is focused on the energy flow through the protein in its folded state. A mathematical model, based on the Brownian motion of coupled harmonic oscillators, is worked out in the appendix.
Customer Reviews:
Reflects Research as of June 2004.......2005-10-28
This book is from a series of lectures given by the author at the Zhou Pei-Yuan Center for Applied Mathematics at Tsinghua University to introduce research in biology to individuals in other sciences.
The first ten chapters are an introduction to statistical physics, but somewhat tilted towards biological applications. The last six chapters cover specific biophysical topics based on the general mathematical/physical principles.
The book introduces an approach to protein folding from the point of view of kinetic theory. This is presented as the driving force of the process. A series of possible research directions is suggested to further investigate these theories.
The book was published in June, 2004 and was up to date with current theories as of that time.
Average customer rating:
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Molecular Chaperones in Health and Disease (Handbook of Experimental Pharmacology) (Handbook of Experimental Pharmacology)
Manufacturer: Springer
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ASIN: 3540258752 |
Product Description
Molecular chaperones are involved in a wide variety of essential cellular processes in living cells. A subset of molecular chaperones have been initially described as heat shock proteins protecting cells from stress damage by keeping cellular proteins in a folding competent state and preventing them from irreversible aggregation. Later it became obvious that molecular chaperones are also expressed constitutively in the cell and are involved in complex processes such as protein synthesis, intracellular protein transport, post-translational modification and secretion of proteins as well as receptor signalling. Hence, it is not surprising that molecular chaperones are implicated in the pathogenesis of many relevant diseases and could be regarded as potential pharmacological targets. Starting with the analysis of the mode of action of chaperones at the molecular, cellular and organismic level, this book will then describe specific aspects where modulation of chaperone action could be of pharmacological and therapeutic interest.
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Prolyl Hydroxylase, Protein Disulfide Isomerase and Other Structurally Related Proteins
Guzman
Manufacturer: CRC
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ASIN: 0824798317 |
Book Description
Addressing the folding of proteins to natural states as well as cotranslational and post translational modifications that effect function, this work analyzes the function of specific enzymes in the complex processes of protein conformation, assembly and stability. It highlights up-to-date advances made in creating accurate protein folding for protein stability, offering results in understanding disease pathology and the development of better drugs.
Customer Reviews:
Great Book !.......2000-08-24
Very good book, everything you need to know about PDI, almost everything...
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Advances in Protein Chemistry, Volume 59: Protein Folding in the Cell (Advances in Protein Chemistry)
Manufacturer: Academic Press
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ASIN: 0120342596 |
Book Description
This volume of
Advances in Protein Chemistry provides a broad, yet deep look at the cellular components that assist protein folding in the cell. This area of research is relatively new--10 years ago these components were barely recognized, so this book is a particularly timely compilation of current information. Topics covered include a review of the structure and mechanism of the major chaperone components, prion formation in yeast, and the use of microarrays in studying stress response. Outlines preceding each chapter allow the reader to quickly access the subjects of greatest interest. The information presented in this book should appeal to biochemists, cell biologists, and structural biologists.
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Misbehaving Proteins: Protein (Mis)Folding, Aggregation, and Stability
Manufacturer: Springer
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Binding: Hardcover
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ASIN: 0387305084 |
Book Description
This text provides an up-to-date collection of theoretical and experimental studies into protein folding, misfolding, aggregation, and stability. Additionally, issues faced during the development of protein products are illustrated. The first section of contributed papers covers advances in computational efforts to examine protein aggregation. In the middle section, several leading researchers describe fundamental experimental efforts to explore the relationships between protein sequence, folded structure, aggregation kinetics, and aggregate morphology. In the final part of the book, contributors discuss the practical issues arising during product development efforts because of the propensity for engineered proteins to misfold and aggregate.
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Protein Folding Protocols (Methods in Molecular Biology)
Manufacturer: Humana Press
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Protein Engineering Protocols (Methods in Molecular Biology)
ASIN: 1588296229 |
Book Description
Protein Folding Protocols presents protocols for studying and characterizing protein folding from the unfolded to the folded state. Covering experiment and theory, bioinformatics approaches, and state-of-the-art simulation protocols for better sampling of the conformational space, this volume describes a broad range of techniques to study, predict, and analyze the protein folding process.
Protein Folding Protocols also provides sample approaches toward the prediction of protein structure starting from the amino acid sequence, in the absence of overall homologous sequences. These approaches have tremendous implications, ranging from drug design, functional assignment, comprehension of the nature of regulation, understanding molecular machines, viral entry into cells, and putting together cellular pathways and their dynamics.
The protocols follow the successful Methods in Molecular Biology™ series format, each one offering step-by-step laboratory instructions, an introduction outlining the principle behind the technique, lists of equipment and reagents, and tips on troubleshooting and avoiding known pitfalls.
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