Items related to Protein Folding Handbook 5-volume set
How a polypeptide chain folds into a stable and functional protein is probably the most important question in present-day molecular biology. Reliably predicting the folding process allows to deduce protein function from genomic information alone and will bring about a revolution in structural genomics. Understanding the way in which proper protein folding is controlled by the cell is required to find a cure for Alzheimer's and other diseases caused by misfolded proteins.
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.
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.
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From the Back Cover:
Based on the expertise of more than 60 research groups from around the globe, this unique reference integrates theoretical, biophysical, biochemical and medical aspects of protein folding for an in-depth coverage of the entire field.
Part I
Principles of Protein Stability
Kinetics of Protein Folding
Folding of Membrane Proteins
Structure and Dynamics of Unfolded States
Folding Intermediates
Molecular Dynamics Simulations of Protein Folding
Part II
In vivo Study of Protein Folding
Cellular Function and Regulation of Chaperones
Misfolded Proteins and Prions
Protein Folding Diseases
Design of Stable Proteins
Biotechnology of Protein Folding
Throughout the book, theoretical as well as practical aspects are addressed, including detailed protocols for key techniques in protein folding research.
The comprehensiveness and outstanding quality of the carefully selected contributions render this the ultimate resource for every scientist with an interest in protein folding.
About the Author:
Part I
Principles of Protein Stability
Kinetics of Protein Folding
Folding of Membrane Proteins
Structure and Dynamics of Unfolded States
Folding Intermediates
Molecular Dynamics Simulations of Protein Folding
Part II
In vivo Study of Protein Folding
Cellular Function and Regulation of Chaperones
Misfolded Proteins and Prions
Protein Folding Diseases
Design of Stable Proteins
Biotechnology of Protein Folding
Throughout the book, theoretical as well as practical aspects are addressed, including detailed protocols for key techniques in protein folding research.
The comprehensiveness and outstanding quality of the carefully selected contributions render this the ultimate resource for every scientist with an interest in protein folding.
Johannes Buchner holds the chair of Biotechnology at the Technical University of Munich (Germany). He studied Biology at the University of Regensburg and afterwards joined the group of Ira Pastan at the National Cancer Institute in Bethesda (United States). Returning to Germany, he took a up junior group leader position at Regensburg before becoming full professor at Munich in 1998.
Professor Buchner's research is centered on the folding process of proteins and its efficiency in vitro and in vivo. To improve the efficiency of protein production, he has pioneered the biotechnological use of chaperones and holds several patents in this area of research.
Thomas Kiefhaber is Professor of Biophysical Chemistry at the Biozentrum, University of Basel (Switzerland). He studied Biology at the University of Regensburg (Germany) and, after completing his PhD in Biophysical Chemistry, spent two years as a post-doc with R. L. Baldwin at Stanford University. Since 1993 he is a member of the faculty of Basel University and was named professor for Biophysical Chemistry in 1999.
Professor Kiefhaber's research is centered on the investigation of kinetics and mechanism of protein folding with biophysical methods.
Professor Buchner's research is centered on the folding process of proteins and its efficiency in vitro and in vivo. To improve the efficiency of protein production, he has pioneered the biotechnological use of chaperones and holds several patents in this area of research.
Thomas Kiefhaber is Professor of Biophysical Chemistry at the Biozentrum, University of Basel (Switzerland). He studied Biology at the University of Regensburg (Germany) and, after completing his PhD in Biophysical Chemistry, spent two years as a post-doc with R. L. Baldwin at Stanford University. Since 1993 he is a member of the faculty of Basel University and was named professor for Biophysical Chemistry in 1999.
Professor Kiefhaber's research is centered on the investigation of kinetics and mechanism of protein folding with biophysical methods.
"About this title" may belong to another edition of this title.
- PublisherWiley-VCH
- Publication date2005
- ISBN 10 3527307842
- ISBN 13 9783527307845
- BindingHardcover
- Edition number1
- Number of pages2623
- EditorBuchner Johannes, Kiefhaber Thomas
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Protein Folding Handbook // VOLUME 3 of 5
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Book Description Hardcover. Condition: New. Volume 3 of the 5-volume set, lxiii + 458 pages, issued without a dust jacket. Weight 1.13kg (please note: extra shipping will be required). New/unused, still sealed in publisher's original shrinkwrap. -- Contents: Part II, Volume 1 -- 1 Paradigm Changes from 'Unboiling an Egg' to 'Synthesizing a Rabbit' / Rainer Jaenicke [Protein Structure, Stability, and Self-organization; Autonomous and Assisted Folding and Association; Native, Intermediate, and Denatured States; Folding and Merging of Domains: Association of Subunits; Limits of Reconstitution; In Vitro Denaturation-Renaturation vs. Folding in Vivo; Perspectives] 2 Folding and Association of Multi-domain and Oligomeric Proteins / Hauke Lilie & Robert Seckler [Folding of Multi-domain Proteins; Folding and Association of Oligomeric Proteins; Renaturation versus Aggregation; Case Studies on Protein Folding and Association; Experimental Protocols] 3 Studying Protein Folding in Vivo / I. Marije Liscaljet [General Features in Folding Proteins Amenable to in Vivo Study; Location-specific Features in Protein Folding; How to Manipulate Protein Folding; Experimental Protocols] 4 Characterization of ATPase Cycles of Molecular Chaperones by Fluorescence and Transient Kinetic Methods / Sandra Schlee & Jochen Reinstein [Characterization of ATPase Cycles of Molecular Chaperones; Experimental Protocols] 5 Analysis of Chaperone Function in Vitro / Johannes Buchner & Stefan Walter [Basic Functional Principles of Molecular Chaperones; Limits and Extensions of the Chaperone Concept; Working with Molecular Chaperones; Assays to Assess and Characterize Chaperone Function; Experimental Protocols] 6 Physical Methods for Studies of Fiber Formation and Structure / Thomas Scheibel & Louise Serpell [Overview: Protein Fibers Formed in Vivo (Amyloid Fibers; Silks; Collagens; Actin, Myosin, and Tropomyosin Filaments; Intermediate Filaments/Nuclear Lamina; Fibrinogen/Fibrin; Microtubules; Elastic Fibers; Flagella and Pili; Filamentary Structures in Rod-like Viruses; Protein Fibers Used by Viruses and Bacteriophages to Bind to Their Hosts); Overview: Fiber Structures; Methods to Study Fiber Assembly; Methods to Study Fiber Morphology and Structure; Concluding Remarks] 7 Protein Unfolding in the Cell / Prakash Koodathingal [Protein Translocation Across Membranes; Protein Unfolding and Degradation by ATP-dependent Proteases; Conclusions; Experimental Protocols] 8 Natively Disordered Proteins / Gary W. Daughdrill [Methods Used to Characterize Natively Disordered Proteins; Do Natively Disordered Proteins Exist Inside Cells (Evolution of Ordered and Disordered Proteins Is Fundamentally Different; Direct Measurement by NMR); Functional Repertoire; Importance of Disorder for Protein Folding; Experimental Protocols] 9 Catalysis of Disulfide Bond Formation in Prokaryotes / Jean-Francois Collet & James C. Bardwell [Disulfide Bond Formation in the E. coli Periplasm; Disulfide Bond Isomerization; Experimental Protocols] 10 Catalysis of Peptidyl-prolyl cis/trans Isomerization by Enzymes / Gunter Fischer [Peptidyl-prolyl cis/trans Isomerization; Monitoring Peptidyl-prolyl cis/trans Isomerase Activity; Prototypical Peptidyl-prolyl cis/trans Isomerases; Concluding Remarks; Experimental Protocols] 11 Secondary Amide Peptide Bond cis/trans Isomerization in Polypeptide Backbone Restructuring: Implications for Catalysis / Cordelia Schiene-Fischer [Monitoring Secondary Amide Peptide Bond cis/trans Isomerization; Kinetics and Thermodynamics of Secondary Amide Peptide Bond cis/trans Isomerization; Principles of DnaK Catalysis; Experimental Protocols] 12 Ribosome-associated Proteins Acting on Newly Synthesized Polypeptide Chains / Sabine Rospert [Signal Recognition Particle, Nascent Polypeptide?associated Complex, and Trigger Factor; Chaperones Bound to the Eukaryotic Ribosome: Hsp70 & Hsp40 Systems; Enzymes Acting on Nascent Polypeptide Chains; Complex Arrangement at the Yeast Ribosomal Tunnel Exit; Experimental Protocols]. Seller Inventory # 007671
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Protein Folding Handbook
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John Wiley & Sons
(2005)
ISBN 10: 3527307842
ISBN 13: 9783527307845
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Protein Folding Handbook
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John Wiley & Sons
(2005)
ISBN 10: 3527307842
ISBN 13: 9783527307845
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PROTEIN FOLDING HANDBOOK (5 VOL.SET)
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Book Description Condition: Brand New. New. US edition. Expediting shipping for all USA and Europe orders excluding PO Box. Excellent Customer Service. Seller Inventory # ABEOCT23-256090
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