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Author : Anne Gershenson
Publisher :
ISBN 13 :
Total Pages : 306 pages
Book Rating : 4.3/5 (91 download)
Download or read book Time Resolved Optical Methods for the Study of Protein Folding and Conformation written by Anne Gershenson and published by . This book was released on 1996 with total page 306 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Author : Bengt Nölting
Publisher : Springer Science & Business Media
ISBN 13 : 354027278X
Total Pages : 222 pages
Book Rating : 4.5/5 (42 download)
Download or read book Protein Folding Kinetics written by Bengt Nölting and published by Springer Science & Business Media. This book was released on 2005-12-05 with total page 222 pages. Available in PDF, EPUB and Kindle. Book excerpt: First methods book which includes many detailed descriptions Absolutely needed and thus timely for the scientific community Comprises 15% more content and includes the mentioned special features
Author : Heinz Fabian
Publisher : Springer Science & Business Media
ISBN 13 : 3642222307
Total Pages : 257 pages
Book Rating : 4.6/5 (422 download)
Download or read book Protein Folding and Misfolding written by Heinz Fabian and published by Springer Science & Business Media. This book was released on 2011-09-18 with total page 257 pages. Available in PDF, EPUB and Kindle. Book excerpt: Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events in the broad arsenal of techniques conventionally used in this field. The progress in understanding protein folding and misfolding is primarily due to the development of biophysical methods which permit to probe conformational changes with high kinetic and structural resolution. The most commonly used approaches rely on rapid mixing methods to initiate the folding event via a sudden change in solvent conditions. Traditionally, techniques such as fluorescence, circular dichroism or visible absorption are applied to probe the process. In contrast to these techniques, infrared spectroscopy came into play only very recently, and the progress made in this field up to date which now permits to probe folding events over the time scale from picoseconds to minutes has not yet been discussed in a book. The aim of this book is to provide an overview of the developments as seen by some of the main contributors to the field. The chapters are not intended to give exhaustive reviews of the literature but, instead to illustrate examples demonstrating the sort of information, which infrared techniques can provide and how this information can be extracted from the experimental data. By discussing the strengths and limitations of the infrared approaches for the investigation of folding and misfolding mechanisms this book helps the reader to evaluate whether a particular system is appropriate for studies by infrared spectroscopy and which specific advantages the techniques offer to solve specific problems.
Author : Jeffrey Alan Stevens
Publisher :
ISBN 13 :
Total Pages : 147 pages
Book Rating : 4.:/5 (719 download)
Download or read book Time Resolved Femtosecond Optical Studies of Heme Proteins Myoglobin and Cytochrome C written by Jeffrey Alan Stevens and published by . This book was released on 2011 with total page 147 pages. Available in PDF, EPUB and Kindle. Book excerpt: Abstract: Our goal was to develop methods to study protein dynamics on the picosecond to nanosecond time scale. We used wavelength and femtosecond resolved fluorescence and absorbance spectroscopy coupled with site-directed mutagenesis to study the heme proteins myoglobin and cytochrome c and determine protein dynamics occurring on the picosecond to nanosecond time scale. The intrinsic amino acid tryptophan was used as a local optical probe and placed one at a time with site-directed mutagenesis that allowed us to achieve a spatial resolution down to a single amino acid. We systematically characterized resonance energy transfer (RET) between a single tryptophan and the prosthetic heme group in myoglobin to develop a novel energy-transfer pair as a molecular ruler in heme proteins to study local conformation fluctuations. Using site-directed mutagenesis, we placed a single tryptophan throughout myoglobin. We observed picosecond RET in tens to hundreds of picoseconds. We also characterized steady state parameters associated with RET allowing us to determine the orientation factor between tryptophan and heme and thus examine changes at different mutation sites revealing relative local structure flexibility and conformation fluctuations. Additionally, local environment relaxation occurs on similar time scales as the RET dynamics, resulting in a nonequilibrium dynamic process. We were able to determine the time scales of such nonequilibrium energy-transfer dynamics and elucidate the mechanism of the nonexponential RET dynamics caused by local dynamic heterogeneity and/or local environment relaxation. In cytochrome c, RET between the lone intrinsic tryptophan and heme was used to study protein folding/unfolding for various states (ferric, ferrous and CO-bound ferrous) of cytochrome c. We systematic studied heme dynamics and induced protein conformational relaxations in cytochrome c and myoglobin with femtosecond transient absorption (TA). A wide range of probing wavelengths from the visible to the UV was probed to unambiguously determine the protein dynamics of the ferric and ferrous state of cytochrome c. For cytochrome c in the ferrous state, the heme undergoes ligand bond breaking and rebinding process generating proteinquakes that perturb the local heme site and shake global protein conformation which was detected by the nearby lone intrinsic tryptophan. Cytochrome c in the ferric state has dynamics that mainly occur at the local site, including ultrafast internal conversion, vibrational cooling, and complete ground-state recovery with no global conformation relaxation observed. We expanded our studies by coupling site-directed mutagenesis of tryptophan at various locations throughout cytochrome c utilizing TA studies. Ligand photolysis from heme was used to generate proteinquakes perturbing the local heme site and shakes global protein conformation and was observed by several of the tryptophan mutations. Additionally, we observed the protein dynamics as a function of denaturing agent. The region that we studied was the pre-unfolding transition region; hence the protein was "softened." In myoglobin, we similarly characterized the heme dynamics of the ferric, ferrous and CO-bound ferrous states. We attempted to use tryptophan as a local probe of protein dynamics for CO-bound myoglobin, but concluded that the perturbation created by CO photolysis was much smaller compared to the proteinquake generated in cytochrome c.
Author : Yawen Bai
Publisher : Springer Science & Business Media
ISBN 13 : 1597451894
Total Pages : 332 pages
Book Rating : 4.5/5 (974 download)
Download or read book Protein Folding Protocols written by Yawen Bai and published by Springer Science & Business Media. This book was released on 2008-02-04 with total page 332 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Author : Richard A. Friesner
Publisher : John Wiley & Sons
ISBN 13 : 0471465232
Total Pages : 544 pages
Book Rating : 4.4/5 (714 download)
Download or read book Computational Methods for Protein Folding, Volume 120 written by Richard A. Friesner and published by John Wiley & Sons. This book was released on 2004-04-07 with total page 544 pages. Available in PDF, EPUB and Kindle. Book excerpt: Since the first attempts to model proteins on a computer began almost thirty years ago, our understanding of protein structure and dynamics has dramatically increased. Spectroscopic measurement techniques continue to improve in resolution and sensitivity, allowing a wealth of information to be obtained with regard to the kinetics of protein folding and unfolding, and complementing the detailed structural picture of the folded state. Concurrently, algorithms, software, and computational hardware have progressed to the point where both structural and kinetic problems may be studied with a fair degree of realism. Despite these advances, many major challenges remain in understanding protein folding at both the conceptual and practical levels. Computational Methods for Protein Folding seeks to illuminate recent advances in computational modeling of protein folding in a way that will be useful to physicists, chemists, and chemical physicists. Covering a broad spectrum of computational methods and practices culled from a variety of research fields, the editors present a full range of models that, together, provide a thorough and current description of all aspects of protein folding. A valuable resource for both students and professionals in the field, the book will be of value both as a cutting-edge overview of existing information and as a catalyst for inspiring new studies. Computational Methods for Protein Folding is the 120th volume in the acclaimed series Advances in Chemical Physics, a compilation of scholarly works dedicated to the dissemination of contemporary advances in chemical physics, edited by Nobel Prize-winner Ilya Prigogine.
Author : Ke-li Han
Publisher : Springer Science & Business Media
ISBN 13 : 3319029703
Total Pages : 488 pages
Book Rating : 4.3/5 (19 download)
Download or read book Protein Conformational Dynamics written by Ke-li Han and published by Springer Science & Business Media. This book was released on 2014-01-20 with total page 488 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book discusses how biological molecules exert their function and regulate biological processes, with a clear focus on how conformational dynamics of proteins are critical in this respect. In the last decade, the advancements in computational biology, nuclear magnetic resonance including paramagnetic relaxation enhancement, and fluorescence-based ensemble/single-molecule techniques have shown that biological molecules (proteins, DNAs and RNAs) fluctuate under equilibrium conditions. The conformational and energetic spaces that these fluctuations explore likely contain active conformations that are critical for their function. More interestingly, these fluctuations can respond actively to external cues, which introduces layers of tight regulation on the biological processes that they dictate. A growing number of studies have suggested that conformational dynamics of proteins govern their role in regulating biological functions, examples of this regulation can be found in signal transduction, molecular recognition, apoptosis, protein / ion / other molecules translocation and gene expression. On the experimental side, the technical advances have offered deep insights into the conformational motions of a number of proteins. These studies greatly enrich our knowledge of the interplay between structure and function. On the theoretical side, novel approaches and detailed computational simulations have provided powerful tools in the study of enzyme catalysis, protein / drug design, protein / ion / other molecule translocation and protein folding/aggregation, to name but a few. This work contains detailed information, not only on the conformational motions of biological systems, but also on the potential governing forces of conformational dynamics (transient interactions, chemical and physical origins, thermodynamic properties). New developments in computational simulations will greatly enhance our understanding of how these molecules function in various biological events.
Author : William W. Parson
Publisher : Springer Nature
ISBN 13 : 3031172221
Total Pages : 653 pages
Book Rating : 4.0/5 (311 download)
Download or read book Modern Optical Spectroscopy written by William W. Parson and published by Springer Nature. This book was released on 2023-02-28 with total page 653 pages. Available in PDF, EPUB and Kindle. Book excerpt: The 3rd edition of this textbook offers clear explanations of optical spectroscopic phenomena and shows how spectroscopic techniques are used in modern chemistry, biochemistry and biophysics. Topics included are: electronic and vibrational absorption fluorescence symmetry operations and normal-mode calculations electron transfer from excited molecules energy transfer exciton interactions electronic and vibrational circular dichroism coherence and dephasing ultrafast pump-probe and photon-echo spectroscopy single-molecule and fluorescence-correlation spectroscopy Raman scattering multiphoton absorption quantum optics and non-linear optics entropy changes during photoexcitation electronic and vibrational Stark effects studies of fast processes in single molecules two-dimensional electronic and vibrational spectroscopy This revised and updated edition provides expanded discussions of laser spectroscopy, crystal symmetry, birefringence, non-linear optics, solar cells and light-emitting diodes. The explanations are sufficiently thorough and detailed to be useful for researchers, graduate students and advanced undergraduates in chemistry, biochemistry and biophysics. They are based on time-dependent quantum mechanics, but are developed from first principles so that they can be understood by readers with little prior training in the field. Additional topics and highlights are presented in special boxes in the text. The book is richly illustrated with color figures throughout. Each chapter ends with a section of questions for self-examination.
Author :
Publisher :
ISBN 13 :
Total Pages : 776 pages
Book Rating : 4.3/5 (91 download)
Download or read book American Doctoral Dissertations written by and published by . This book was released on 2002 with total page 776 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Author : Roger L. Lundblad
Publisher : CRC Press
ISBN 13 : 1351680536
Total Pages : 551 pages
Book Rating : 4.3/5 (516 download)
Download or read book Biochemistry and Molecular Biology Compendium written by Roger L. Lundblad and published by CRC Press. This book was released on 2019-11-11 with total page 551 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book is an accessible resource offering practical information not found in more database-oriented resources. The first chapter lists acronyms with definitions, and a glossary of terms and subjects used in biochemistry, molecular biology, biotechnology, proteomics, genomics, and systems biology. There follows chapters on chemicals employed in biochemistry and molecular biology, complete with properties and structure drawings. Researchers will find this book to be a valuable tool that will save them time, as well as provide essential links to the roots of their science. Key selling features: Contains an extensive list of commonly used acronyms with definitions Offers a highly readable glossary for systems and techniques Provides comprehensive information for the validation of biotechnology assays and manufacturing processes Includes a list of Log P values, water solubility, and molecular weight for selected chemicals Gives a detailed listing of protease inhibitors and cocktails, as well as a list of buffers
Author : 劉鎮宇
Publisher :
ISBN 13 :
Total Pages : 66 pages
Book Rating : 4.:/5 (442 download)
Download or read book The Use of Time-resolved Fluorescence Spectroscopy and the Synthesis of a New Photolabile Linker to Study Protein Folding written by 劉鎮宇 and published by . This book was released on 2000 with total page 66 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Author : Heinz Fabian
Publisher : Springer
ISBN 13 : 9783642222313
Total Pages : 244 pages
Book Rating : 4.2/5 (223 download)
Download or read book Protein Folding and Misfolding written by Heinz Fabian and published by Springer. This book was released on 2011-09-22 with total page 244 pages. Available in PDF, EPUB and Kindle. Book excerpt: Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events in the broad arsenal of techniques conventionally used in this field. The progress in understanding protein folding and misfolding is primarily due to the development of biophysical methods which permit to probe conformational changes with high kinetic and structural resolution. The most commonly used approaches rely on rapid mixing methods to initiate the folding event via a sudden change in solvent conditions. Traditionally, techniques such as fluorescence, circular dichroism or visible absorption are applied to probe the process. In contrast to these techniques, infrared spectroscopy came into play only very recently, and the progress made in this field up to date which now permits to probe folding events over the time scale from picoseconds to minutes has not yet been discussed in a book. The aim of this book is to provide an overview of the developments as seen by some of the main contributors to the field. The chapters are not intended to give exhaustive reviews of the literature but, instead to illustrate examples demonstrating the sort of information, which infrared techniques can provide and how this information can be extracted from the experimental data. By discussing the strengths and limitations of the infrared approaches for the investigation of folding and misfolding mechanisms this book helps the reader to evaluate whether a particular system is appropriate for studies by infrared spectroscopy and which specific advantages the techniques offer to solve specific problems.
Author :
Publisher : Academic Press
ISBN 13 : 0080957188
Total Pages : 3533 pages
Book Rating : 4.0/5 (89 download)
Download or read book Comprehensive Biophysics written by and published by Academic Press. This book was released on 2012-04-12 with total page 3533 pages. Available in PDF, EPUB and Kindle. Book excerpt: Biophysics is a rapidly-evolving interdisciplinary science that applies theories and methods of the physical sciences to questions of biology. Biophysics encompasses many disciplines, including physics, chemistry, mathematics, biology, biochemistry, medicine, pharmacology, physiology, and neuroscience, and it is essential that scientists working in these varied fields are able to understand each other's research. Comprehensive Biophysics, Nine Volume Set will help bridge that communication gap. Written by a team of researchers at the forefront of their respective fields, under the guidance of Chief Editor Edward Egelman, Comprehensive Biophysics, Nine Volume Set provides definitive introductions to a broad array of topics, uniting different areas of biophysics research - from the physical techniques for studying macromolecular structure to protein folding, muscle and molecular motors, cell biophysics, bioenergetics and more. The result is this comprehensive scientific resource - a valuable tool both for helping researchers come to grips quickly with material from related biophysics fields outside their areas of expertise, and for reinforcing their existing knowledge. Biophysical research today encompasses many areas of biology. These studies do not necessarily share a unique identifying factor. This work unites the different areas of research and allows users, regardless of their background, to navigate through the most essential concepts with ease, saving them time and vastly improving their understanding The field of biophysics counts several journals that are directly and indirectly concerned with the field. There is no reference work that encompasses the entire field and unites the different areas of research through deep foundational reviews. Comprehensive Biophysics fills this vacuum, being a definitive work on biophysics. It will help users apply context to the diverse journal literature offering, and aid them in identifying areas for further research Chief Editor Edward Egelman (E-I-C, Biophysical Journal) has assembled an impressive, world-class team of Volume Editors and Contributing Authors. Each chapter has been painstakingly reviewed and checked for consistent high quality. The result is an authoritative overview which ties the literature together and provides the user with a reliable background information and citation resource
Author : Charis Ghelis
Publisher : Academic Press
ISBN 13 : 0323140920
Total Pages : 580 pages
Book Rating : 4.3/5 (231 download)
Download or read book Protein Folding written by Charis Ghelis and published by Academic Press. This book was released on 2012-12-02 with total page 580 pages. Available in PDF, EPUB and Kindle. Book excerpt: Protein Folding aims to collect the most important information in the field of protein folding and probes the main principles that govern formation of the three-dimensional structure of a protein from a nascent polypeptide chain, as well as how the functional properties appear. This text is organized into three sections and consists of 15 chapters. After an introductory chapter where the main problems of protein folding are considered at the cellular level in the context of protein biosynthesis, the discussion turns to the conformation of native globular proteins. Definitions and rules of nomenclature are given, including the structural organization of globular proteins deduced from X-ray crystallographic data. Folding mechanisms are tentatively deduced from the observation of invariants in the architecture of folded proteins. The next chapters focus on the energetics of protein conformation and structure, indicating the principles of thermodynamic stability of the native structure, along with theoretical computation studies of protein folding, structure prediction, and folding simulation. The reader is also introduced to various experimental approaches; the reversibility of the unfolding-folding process; equilibrium and kinetic studies; and detection and characterization of intermediates in protein folding. This text concludes with a chapter dealing with problems specific to oligomeric proteins. This book is intended for research scientists, specialists, biochemists, and students of biochemistry and biology.
Author : G.D. Fasman
Publisher : Springer Science & Business Media
ISBN 13 : 1475725086
Total Pages : 739 pages
Book Rating : 4.4/5 (757 download)
Download or read book Circular Dichroism and the Conformational Analysis of Biomolecules written by G.D. Fasman and published by Springer Science & Business Media. This book was released on 2013-11-11 with total page 739 pages. Available in PDF, EPUB and Kindle. Book excerpt: ''Excellent and very timely....It will undoubtedly become a standard reference for the application of circular dichroism (CD) to biomolecules.'' --- Quarterly Review of Biology, March 1997 ''[T]estament to the book's utility is the fact that during the course of my review I had to 'rescue' it from the desks of graduate students on an almost daily basis. In summary, this is a great book.'' --- American Scientist ''Well documented chapters provide a very good insight into the problems surrounding the conformation of biomacromolecules...An indispensible source of information.'' --- Nahrung, 42(2), 1998 Renowned experts present the first state-of-the-art description of circular dichroism spectroscopy (CD). Chapters present in-depth discussions of the history of the field, the theory of CD for application to globular proteins, membrane proteins, peptides, nucleic acids and their interactions, carbohydrates, and instrumentation. Discussions also feature new techniques using synchrotron radiation, vibrational Raman optical activity, and vibrational CD. More than 250 illustrations supplement the text.
Author : Isabella C. Felli
Publisher : Springer
ISBN 13 : 3319201646
Total Pages : 428 pages
Book Rating : 4.3/5 (192 download)
Download or read book Intrinsically Disordered Proteins Studied by NMR Spectroscopy written by Isabella C. Felli and published by Springer. This book was released on 2015-09-19 with total page 428 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book discusses the paradigm-shifting phenomenon of intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered domains and functional IDP regions (IDPRs). The properties of IDPs and IDPRs are highly complementary to those deriving from the presence of a unique and well-defined three-dimensional fold. Ignored for a long time in high-resolution studies of proteins, intrinsic protein disorder is now recognized as one of the key features for a large variety of cellular functions, where structural flexibility presents a functional advantage in terms of binding plasticity and promiscuity and this volume explores this exciting new research. Recent progress in the field has radically changed our perspective to study IDPs through NMR: increasingly complex IDPs can now be characterized, a wide range of observables can be determined reporting on the structural and dynamic properties, computational methods to describe the structure and dynamics are in continuous development and IDPs can be studied in environments as complex as whole cells. This volume communicates the new exciting possibilities offered by NMR and presents open questions to foster further developments. Intrinsically Disordered Proteins Studied by NMR Spectroscopy provides a snapshot to researchers entering the field as well as providing a current overview for more experienced scientists in related areas.
Author : Hui Lu
Publisher :
ISBN 13 :
Total Pages : 440 pages
Book Rating : 4.:/5 (535 download)
Download or read book Studies of Protein Folding and Unfolding Using NMR and Optical Methods written by Hui Lu and published by . This book was released on 1996 with total page 440 pages. Available in PDF, EPUB and Kindle. Book excerpt:
