Protein Ligand Binding Thermodynamics

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Protein–Ligand Binding Thermodynamics

Author : Justin M. Miller,Justin D. Marsee
Publisher : American Chemical Society
Page : 217 pages
File Size : 50,9 Mb
Release : 2023-06-01
Category : Science
ISBN : 9780841299795

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Protein–Ligand Binding Thermodynamics by Justin M. Miller,Justin D. Marsee Pdf

Ligand binding by macromolecules represents a core event of broad relevance to a range of systems, including catalytic systems alongside noncatalytic systems such as nucleic acid binding by transcription factors or extracellular ligand binding by proteins involved in signaling pathways. The scope of this primer is constrained to introduce only foundational models without significant discussion of more advanced topics such as allosteric or linkage effects. Linkage occurs when the binding of a ligand is influenced by the binding of another molecule of the same ligand (homotropic linkage), the binding of a different ligand (heterotropic linkage), physical variables such as temperature or pressure (physical linkage), or changes in macromolecular assembly state (polysteric linkage). Taking this into account, the foundational themes presented in this primer can be used to describe any macromolecule–ligand interaction either by direct use of the models and techniques described here or by applying them to develop more advanced models to explain additional complexities such as those allosteric or linkage effects just mentioned. The target audience of this primer is the senior undergraduate or junior graduate student who lacks a foundation in ligand-binding thermodynamics. As such, we have focused primarily on foundational thermodynamic treatments and presented only general discussions of relevant experimental designs. Readers of this primer will learn how to build a working understanding of common factors that promote energetic favorability for ligand binding; develop a functional toolbox to understand ligand binding from the perspective of collecting, plotting, and interpreting ligand-binding data; enhance proficiency in deriving thermodynamic mechanisms for ligand binding; and become comfortable in interpreting binding data reported in the literature and independently expanding knowledge beyond the scope introduced in this primer.

Frontiers in Protein Structure, Function, and Dynamics

Author : Dev Bukhsh Singh,Timir Tripathi
Publisher : Springer Nature
Page : 458 pages
File Size : 44,5 Mb
Release : 2020-07-02
Category : Science
ISBN : 9789811555305

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Frontiers in Protein Structure, Function, and Dynamics by Dev Bukhsh Singh,Timir Tripathi Pdf

This book discusses a broad range of basic and advanced topics in the field of protein structure, function, folding, flexibility, and dynamics. Starting with a basic introduction to protein purification, estimation, storage, and its effect on the protein structure, function, and dynamics, it also discusses various experimental and computational structure determination approaches; the importance of molecular interactions and water in protein stability, folding and dynamics; kinetic and thermodynamic parameters associated with protein-ligand binding; single molecule techniques and their applications in studying protein folding and aggregation; protein quality control; the role of amino acid sequence in protein aggregation; muscarinic acetylcholine receptors, antimuscarinic drugs, and their clinical significances. Further, the book explains the current understanding on the therapeutic importance of the enzyme dopamine beta hydroxylase; structural dynamics and motions in molecular motors; role of cathepsins in controlling degradation of extracellular matrix during disease states; and the important structure-function relationship of iron-binding proteins, ferritins. Overall, the book is an important guide and a comprehensive resource for understanding protein structure, function, dynamics, and interaction.

Protein-Ligand Interactions

Author : Holger Gohlke
Publisher : John Wiley & Sons
Page : 361 pages
File Size : 43,6 Mb
Release : 2012-05-21
Category : Medical
ISBN : 9783527329663

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Protein-Ligand Interactions by Holger Gohlke Pdf

Innovative and forward-looking, this volume focuses on recent achievements in this rapidly progressing field and looks at future potential for development. The first part provides a basic understanding of the factors governing protein-ligand interactions, followed by a comparison of key experimental methods (calorimetry, surface plasmon resonance, NMR) used in generating interaction data. The second half of the book is devoted to insilico methods of modeling and predicting molecular recognition and binding, ranging from first principles-based to approximate ones. Here, as elsewhere in the book, emphasis is placed on novel approaches and recent improvements to established methods. The final part looks at unresolved challenges, and the strategies to address them. With the content relevant for all drug classes and therapeutic fields, this is an inspiring and often-consulted guide to the complexity of protein-ligand interaction modeling and analysis for both novices and experts.

Bioactive Conformation I

Author : Thomas Peters
Publisher : Springer
Page : 309 pages
File Size : 46,7 Mb
Release : 2006-12-08
Category : Science
ISBN : 9783540490784

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Bioactive Conformation I by Thomas Peters Pdf

This series presents critical reviews of the present position and future trends in modern chemical research. It contains short and concise reports on chemistry, each written by the world renowned experts – it is still valid and useful after 5 or 10 years. More information as well as the electronic version of the whole content available at: springerlink.com. The book will appeal to scientists and practitioners in the mentioned fields and in industry.

Proteomics and Protein-Protein Interactions

Author : Gabriel Waksman
Publisher : Springer Science & Business Media
Page : 325 pages
File Size : 47,8 Mb
Release : 2006-12-22
Category : Medical
ISBN : 9780387245324

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Proteomics and Protein-Protein Interactions by Gabriel Waksman Pdf

Gabriel Waksman Institute of Structural Molecular Biology, Birkbeck and University College London, Malet Street, London WC1E 7HX, United Kingdom Address for correspondence: Professor Gabriel Waksman Institute of Structural Molecular Biology Birkbeck and University College London Malet Street London WC1E 7H United Kingdom Email: g. waksman@bbk. ac. uk and g. waksman@ucl. ac. uk Phone: (+44) (0) 207 631 6833 Fax: (+44) (0) 207 631 6833 URL: http://people. cryst. bbk. ac. uk/?ubcg54a Gabriel Waksman is Professor of Structural Molecular Biology at the Institute of Structural Molecular Biology at UCL/Birkbeck, of which he is also the director. Before joining the faculty of UCL and Birkbeck, he was the Roy and Diana Vagelos Professor of Biochemistry and Molecular Biophysics at the Washington University School of Medicine in St Louis (USA). The rapidly evolving ?eld of protein science has now come to realize the ubiquity and importance of protein–protein interactions. It had been known for some time that proteins may interact with each other to form functional complexes, but it was thought to be the property of only a handful of key proteins. However, with the advent of hi- throughput proteomics to monitor protein–protein interactions at an organism level, we can now safely state that protein–protein interactions are the norm and not the exception.

Microcalorimetry of Biological Molecules

Author : Eric Ennifar
Publisher : Humana
Page : 0 pages
File Size : 51,8 Mb
Release : 2019-04-01
Category : Science
ISBN : 1493991787

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Microcalorimetry of Biological Molecules by Eric Ennifar Pdf

This volume provides methods on microcalorimetry approaches to investigate complex biological molecular systems. Chapters guide readers through Differential Scanning Calorimetry (DSC), Isothermal Titration Calorimetry (ITC), and advanced data processing. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and practical, Microcalorimetry of Biological Molecules: Methods and Protocols aims to ensure successful results in the further study of this vital field.

Linkage Thermodynamics of Macromolecular Interactions

Author : Anonim
Publisher : Academic Press
Page : 485 pages
File Size : 46,5 Mb
Release : 1998-06-24
Category : Science
ISBN : 9780080582245

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Linkage Thermodynamics of Macromolecular Interactions by Anonim Pdf

This volume commemorates the 50th anniversary of the appearance in Volume 4 in 1948 of Dr. Jeffries Wyman's famous paper in which he "laid down" the foundations of linkage thermodynamics. Experts in this area contribute articles on the state-of-the-art of this important field and on new developments of the original theory. Among the topics covered in this volume are electrostatic contributions to molecular free energies in solution; site-specific analysis of mutational effects in proteins; allosteric transitions of the acetylcholine receptor; and deciphering the molecular code of hemoglobin allostery.

Reversible Ligand Binding

Author : Andrea Bellelli,Jannette Carey
Publisher : John Wiley & Sons
Page : 309 pages
File Size : 49,6 Mb
Release : 2018-01-09
Category : Science
ISBN : 9781119238485

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Reversible Ligand Binding by Andrea Bellelli,Jannette Carey Pdf

Presents the physical background of ligand binding and instructs on how experiments should be designed and analyzed Reversible Ligand Binding: Theory and Experiment discusses the physical background of protein-ligand interactions—providing a comprehensive view of the various biochemical considerations that govern reversible, as well as irreversible, ligand binding. Special consideration is devoted to enzymology, a field usually treated separately from ligand binding, but actually governed by identical thermodynamic relationships. Attention is given to the design of the experiment, which aids in showing clear evidence of biochemical features that may otherwise escape notice. Classical experiments are reviewed in order to further highlight the importance of the design of the experiment. Overall, the book supplies students with the understanding that is necessary for interpreting ligand binding experiments, formulating plausible reaction schemes, and analyzing the data according to the chosen model(s). Topics covered include: theory of ligand binding to monomeric proteins; practical considerations and commonly encountered problems; oligomeric proteins with multiple binding sites; ligand binding kinetics; hemoglobin and its ligands; single-substrate enzymes and their inhibitors; two-substrate enzymes and their inhibitors; and rapid kinetic methods for studying enzyme reactions. Bridges theory of ligand binding and allostery with experiments Applies historical and physical insight to provide a clear understanding of ligand binding Written by a renowned author with long-standing research and teaching expertise in the area of ligand binding and allostery Based on FEBS Advanced Course lectures on the topic Reversible Ligand Binding: Theory and Experiment is an ideal text reference for students and scientists involved in biophysical chemistry, physical biochemistry, biophysics, molecular biology, protein engineering, drug design, pharmacology, physiology, biotechnology, and bioengineering.

Ligand-Receptor Energetics

Author : Irving M. Klotz
Publisher : John Wiley & Sons
Page : 196 pages
File Size : 44,7 Mb
Release : 1997-03-14
Category : Science
ISBN : 0471176265

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Ligand-Receptor Energetics by Irving M. Klotz Pdf

Energetische Wechselbeziehungen zwischen Ligand und Rezeptor sind besonders bei der Wechselwirkung kleiner Moleküle mit größeren unter Bildung komplexer Makromoleküle von Bedeutung, welche eine essentielle Rolle in Chemie, Biochemie, Biophysik, Pharmakologie und vielen anderen Gebieten spielen. Hier werden die thermodynamischen Ansätze experimentell und theoretisch erläutert - mit vielen Illustrationen zur Erklärung der Ligand-Bindungskonzepte.

Protein-Ligand Interactions

Author : Hans-Joachim Böhm,Gisbert Schneider
Publisher : John Wiley & Sons
Page : 262 pages
File Size : 45,9 Mb
Release : 2006-03-06
Category : Science
ISBN : 9783527605514

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Protein-Ligand Interactions by Hans-Joachim Böhm,Gisbert Schneider Pdf

The lock-and-key principle formulated by Emil Fischer as early as the end of the 19th century has still not lost any of its significance for the life sciences. The basic aspects of ligand-protein interaction may be summarized under the term 'molecular recognition' and concern the specificity as well as stability of ligand binding. Molecular recognition is thus a central topic in the development of active substances, since stability and specificity determine whether a substance can be used as a drug. Nowadays, computer-aided prediction and intelligent molecular design make a large contribution to the constant search for, e. g., improved enzyme inhibitors, and new concepts such as that of pharmacophores are being developed. An up-to-date presentation of an eternally young topic, this book is an indispensable information source for chemists, biochemists and pharmacologists dealing with the binding of ligands to proteins.

Fragment-Based Drug Discovery

Author : Steven Howard,Chris Abell
Publisher : Royal Society of Chemistry
Page : 314 pages
File Size : 47,9 Mb
Release : 2015-07-03
Category : Medical
ISBN : 9781849739085

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Fragment-Based Drug Discovery by Steven Howard,Chris Abell Pdf

Fragment-based drug discovery is a rapidly evolving area of research, which has recently seen new applications in areas such as epigenetics, GPCRs and the identification of novel allosteric binding pockets. The first fragment-derived drug was recently approved for the treatment of melanoma. It is hoped that this approval is just the beginning of the many drugs yet to be discovered using this fascinating technique. This book is written from a Chemist's perspective and comprehensively assesses the impact of fragment-based drug discovery on a wide variety of areas of medicinal chemistry. It will prove to be an invaluable resource for medicinal chemists working in academia and industry, as well as anyone interested in novel drug discovery techniques.

Thermodynamics and Kinetics of Drug Binding

Author : György Keserü,David C. Swinney
Publisher : John Wiley & Sons
Page : 360 pages
File Size : 52,7 Mb
Release : 2015-03-09
Category : Medical
ISBN : 9783527673056

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Thermodynamics and Kinetics of Drug Binding by György Keserü,David C. Swinney Pdf

This practical reference for medicinal and pharmaceutical chemists combines the theoretical background with modern methods as well as applications from recent lead finding and optimization projects. Divided into two parts on the thermodynamics and kinetics of drug-receptor interaction, the text provides the conceptual and methodological basis for characterizing binding mechanisms for drugs and other bioactive molecules. It covers all currently used methods, from experimental approaches, such as ITC or SPR, right up to the latest computational methods. Case studies of real-life lead or drug development projects are also included so readers can apply the methods learned to their own projects. Finally, the benefits of a thorough binding mode analysis for any drug development project are summarized in an outlook chapter written by the editors.

Biophysical Approaches Determining Ligand Binding to Biomolecular Targets

Author : Alberto Podjarny,Annick P Dejaegere,Bruno Kieffer
Publisher : Royal Society of Chemistry
Page : 260 pages
File Size : 42,8 Mb
Release : 2011-04-01
Category : Science
ISBN : 9781849732666

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Biophysical Approaches Determining Ligand Binding to Biomolecular Targets by Alberto Podjarny,Annick P Dejaegere,Bruno Kieffer Pdf

The binding of small ligands to biological molecules is central to most aspects of biological function. The past twenty years has seen the development of an increasing armoury of biophysical methods that not only detect such binding, but also provide varying degrees of information about the kinetics, thermodynamics and structural aspects of the process. These methods have received increasing attention with the growth in more rational approaches to drug discovery and design. This book reviews the latest advances in the application of biophysics to the study of ligand binding. It provides a complete overview of current techniques to identify ligands, characterise their binding sites and understand their binding mechanisms. Particular emphasis is given to the combined use of different techniques and their relative strengths and weaknesses. Consistency in the way each technique is described makes it easy for readers to select the most suitable protocol for their research. The introduction explains why some techniques are more suitable than others and emphasizes the possible synergies between them. The following chapters, all written by a specialist in the particular technique, focus on each method individually. The book finishes by describing how several complimentary techniques can be used together for maximum effectiveness. This book is suitable for biomolecular scientists at graduate or post-doctoral level in academia and industry. Biologists and chemists will also find it a useful introduction to the techniques available.

Protein Conformational Dynamics

Author : Ke-li Han,Xin Zhang,Ming-jun Yang
Publisher : Springer Science & Business Media
Page : 488 pages
File Size : 40,5 Mb
Release : 2014-01-20
Category : Medical
ISBN : 9783319029702

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Protein Conformational Dynamics by Ke-li Han,Xin Zhang,Ming-jun Yang Pdf

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.

Protein Interactions

Author : G. Weber
Publisher : Springer
Page : 312 pages
File Size : 51,7 Mb
Release : 1992-05-31
Category : Medical
ISBN : UOM:39015026879240

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Protein Interactions by G. Weber Pdf

A study of the thermodynamics of protein-protein and protein-ligand interactions. The author explains the energetics of protein interactions and gives a thorough account of the complicated biophysics that occur when the effects of multiple, complex molecules are taken into account.