Author: George Lisi
Publisher: Frontiers Media SA
ISBN: 2889748219
Category : Science
Languages : en
Pages : 211

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Book Description

Author: Bruce Alberts
Publisher:
ISBN: 9780815332183
Category : Cytology
Languages : en
Pages : 0

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Book Description

Author: Guang Hu
Publisher: Frontiers Media SA
ISBN: 2889668487
Category : Science
Languages : en
Pages : 276

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Book Description

Author: Aron W. Fenton
Publisher: Humana Press
ISBN: 9781493958641
Category : Science
Languages : en
Pages : 439

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Book Description
Despite considerable variability within the scientific community, allosteric regulation can best be defined functionally as how a macromolecule binds one ligand differently when a second ligand is or is not pre-bound to the macromolecule, which constitutes a vital aspect of protein structure/function. In Allostery: Methods and Protocols, expert researchers in the field provide key techniques to investigate this biological phenomenon. Focusing on heterotropic systems with some coverage of homotropic systems, this volume covers the monitoring of allosteric function, allosteric conformational changes, and allosteric changes in protein dynamics/sub-population distribution, as well as topics such as macromolecular and ligand engineering of allosteric functions and computational aids in the study of allostery. Written in the highly successful Methods in Molecular BiologyTM series format, the chapters include the kind of detailed description and implementation advice that is crucial for getting optimal results in the laboratory. Thorough and intuitive, Allostery: Methods and Protocols aids scientists in continuing to study ligand-induced, through-protein effects on protein function (ligand binding/catalysis), a phenomenon that is well recognized through the history of the life sciences and very poorly understood at the molecular level.

Author: Oleg Jardetzky
Publisher: Springer Science & Business Media
ISBN: 1461548950
Category : Science
Languages : en
Pages : 227

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Book Description
This volume is a collection of articles from the proceedings of the International School of Structural Biology and Magnetic Resonance 3rd Course: Protein Dynamics, Function, and Design. This NATO Advance Study Institute was held in Erice at the Ettore Majorana Centre for Scientific Culture on April 16-28, 1997. The aim of the Institute was to bring together experts applyipg different physical methods to problems of macro molecular dynamics-notably x-ray diffraction, NMR and other forms of spectroscopy, and molecular dynamics simulations. Emphasis was placed on those systems and types of problems-such as mechanisms of allosteric control, signal transmission, induced fit to different ligands with its implications for drug design, and the effects of dynamics on structure determination-where a correlation of findings obtained by different methods could shed the most light on the mechanisms involved and stimulate the search for new approaches. The individual articles represent the state of the art in each of the areas cov ered and provide a guide to the original literature in this rapidly developing field. v CONTENTS 1. Determining Structures of ProteinlDN A Complexes by NMR Angela M. Gronenbom and G. Marius Clore 2. Fitting Protein Structures to Experimental Data: Lessons from before Your Mother Was Born . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 15 Jeffrey C. Hoch, Alan S. Stem, and Peter J. Connolly 3. Multisubunit Allosteric Proteins. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 27 William N. Lipscomb 4. Studying Protein Structure and Function by Directed Evolution: Examples with Engineered Antibodies . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 37 Andreas Pliickthun 5. High Pressure Effects on Protein Structure . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .

Author: Aron W. Fenton
Publisher: Humana Press
ISBN: 9781617793332
Category : Science
Languages : en
Pages : 0

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Book Description
Despite considerable variability within the scientific community, allosteric regulation can best be defined functionally as how a macromolecule binds one ligand differently when a second ligand is or is not pre-bound to the macromolecule, which constitutes a vital aspect of protein structure/function. In Allostery: Methods and Protocols, expert researchers in the field provide key techniques to investigate this biological phenomenon. Focusing on heterotropic systems with some coverage of homotropic systems, this volume covers the monitoring of allosteric function, allosteric conformational changes, and allosteric changes in protein dynamics/sub-population distribution, as well as topics such as macromolecular and ligand engineering of allosteric functions and computational aids in the study of allostery. Written in the highly successful Methods in Molecular BiologyTM series format, the chapters include the kind of detailed description and implementation advice that is crucial for getting optimal results in the laboratory. Thorough and intuitive, Allostery: Methods and Protocols aids scientists in continuing to study ligand-induced, through-protein effects on protein function (ligand binding/catalysis), a phenomenon that is well recognized through the history of the life sciences and very poorly understood at the molecular level.

Author: Jian Zhang
Publisher: Springer Nature
ISBN: 9811387192
Category : Medical
Languages : en
Pages : 384

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Book Description
The book focuses on protein allostery in drug discovery. Allosteric regulation, ʹthe second secret of lifeʹ, fine-tunes virtually most biological processes and controls physiological activities. Allostery can both cause human diseases and contribute to development of new therapeutics. Allosteric drugs exhibit unparalleled advantages compared to conventional orthosteric drugs, rendering the development of allosteric modulators as an appealing strategy to improve selectivity and pharmacodynamic properties in drug leads. The Series delineates the immense significance of protein allostery—as demonstrated by recent advances in the repertoires of the concept, its mechanistic mechanisms, and networks, characteristics of allosteric proteins, modulators, and sites, development of computational and experimental methods to predict allosteric sites, small-molecule allosteric modulators of protein kinases and G-protein coupled receptors, engineering allostery, and the underlying role of allostery in precise medicine. Comprehensive understanding of protein allostery is expected to guide the rational design of allosteric drugs for the treatment of human diseases. The book would be useful for scientists and students in the field of protein science and Pharmacology etc.

Author: Pierre Pontarotti
Publisher: Springer
ISBN: 9783030303655
Category : Science
Languages : en
Pages : 0

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Book Description
This book presents 15 selected contributions to the 22nd Evolutionary Biology Meeting, which took place in September 2018 in Marseille. They are grouped under the following major themes: · Origin of Life · Concepts and Methods · Genome and Phenotype Evolution The aims of these annual meetings in Marseille are to bring together leading evolutionary biologists and other scientists who employ evolutionary biology concepts, e.g. for medical research, and to promote the exchange of ideas and encourage interdisciplinary collaborations. Offering an up-to-date overview of recent advances in the field of evolutionary biology, this book represents an invaluable source of information for scientists, teachers and advanced students.

Author: Jean-Paul Renaud
Publisher: John Wiley & Sons
ISBN: 1118900502
Category : Medical
Languages : en
Pages : 1367

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Book Description
With the most comprehensive and up-to-date overview of structure-based drug discovery covering both experimental and computational approaches, Structural Biology in Drug Discovery: Methods, Techniques, and Practices describes principles, methods, applications, and emerging paradigms of structural biology as a tool for more efficient drug development. Coverage includes successful examples, academic and industry insights, novel concepts, and advances in a rapidly evolving field. The combined chapters, by authors writing from the frontlines of structural biology and drug discovery, give readers a valuable reference and resource that: Presents the benefits, limitations, and potentiality of major techniques in the field such as X-ray crystallography, NMR, neutron crystallography, cryo-EM, mass spectrometry and other biophysical techniques, and computational structural biology Includes detailed chapters on druggability, allostery, complementary use of thermodynamic and kinetic information, and powerful approaches such as structural chemogenomics and fragment-based drug design Emphasizes the need for the in-depth biophysical characterization of protein targets as well as of therapeutic proteins, and for a thorough quality assessment of experimental structures Illustrates advances in the field of established therapeutic targets like kinases, serine proteinases, GPCRs, and epigenetic proteins, and of more challenging ones like protein-protein interactions and intrinsically disordered proteins

Author: Lindsey Denise Handley
Publisher:
ISBN: 9781339091617
Category :
Languages : en
Pages : 143

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Book Description
Allostery is a critical process that allows for the regulation of proteins : binding of a molecule at one distal, functional site in a protein can cause changes to a different functional site. Early on, allostery was described as a change in protein structure upon the binding of another molecule. However, a dynamic model of protein allostery is emerging, which more completely describes allosteric phenomena. This work investigates protein dynamics under the lens of allosteric regulation for two different protein systems : (1) IkappaBalpha and (2) thrombin and its cofactor, thrombomodulin. In Chapter II, we present results from NMR studies which probe the roles of ankyrin repeat consensus mutations in IkappaBalpha. These results reveal that consensus mutations cause long-range, allosteric effects throughout the ankyrin repeat domains, including the ordering of the C-terminal PEST sequence on the ps-ns timescale, which is a region critical for proteosomal degradation. In Chapter III, a new construct of thrombomodulin, named TM456m, is characterized using kinetic protein C activation assays to determine whether the protein is suitable for use in future NMR experiments bound to thrombin. Here, we show that TM456m has tighter binding than the previously studied TM45 and higher stability than full-length TM456. Furthermore, we present the first HSQC of TMbound thrombin and observe allosteric changes across the thrombin molecule. Chapter IV presents a hydrogen-deuterium exchange mass spectrometry study that we performed in order to investigate where changes in solvent accessibility occur in the thrombin molecule when an active site substrate (PPACK) or an effector molecule (TM456m) is bound. In both cases, allosteric changes occurred across the thrombin molecule. This study reveals that N-terminus of the heavy chain of thrombin is not buried in the Ile cleft, contrary to all crystal structures of thrombin to date, and that substrate and TM binding allosterically pull the N-terminus into the Ile cleft. In Chapter V, we assign the amide peaks of apo-thrombin and measure its NMR backbone dynamics. Comparison of PPACK-thrombin chemical shifts and backbone dynamics with those of apo-thrombin reveals that allosteric pathways are inherently built into apo-thrombin and suggests that effector-binding might work via a conformational selection mechanism from a broad selection of conformational states.