Matrix Bound Peptides Modeling Protein-protein Interactions
Author | : Chao Yu |
Publisher | : |
Total Pages | : 234 |
Release | : 2003 |
Genre | : |
ISBN | : |
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Author | : Chao Yu |
Publisher | : |
Total Pages | : 234 |
Release | : 2003 |
Genre | : |
ISBN | : |
Author | : Ora Schueler-Furman |
Publisher | : Methods in Molecular Biology |
Total Pages | : 324 |
Release | : 2019-03-13 |
Genre | : Science |
ISBN | : 9781493983025 |
This volume covers an array of techniques available for studying peptide-protein docking and design. The book is divided into four sections: peptide binding site prediction; peptide-protein docking; prediction and design of peptide binding specificity; and the design of inhibitory peptides. The chapters in Modeling Peptide-Protein Interactions: Methods and Protocols cover topics such as the usage of ACCLUSTER and PeptiMap for peptide binding site prediction; AnchorDock and ATTRACT for blind, flexible docking of peptides to proteins; flexible peptide docking using HADDOCK and FlexPepDock; identifying loop-mediated protein-protein interactions using LoopFinder; and protein-peptide interaction design using PinaColada. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary details for successful application of the different approaches and step-by-step, readily reproducible protocols, as well as tips on troubleshooting and avoiding known pitfalls. Cutting-edge and thorough, Modeling Peptide-Protein Interactions: Methods and Protocols provides a diverse and unified overview of this rapidly advancing field of major interest and applicability.
Author | : Bruce Alberts |
Publisher | : |
Total Pages | : 0 |
Release | : 2002 |
Genre | : Cytology |
ISBN | : 9780815332183 |
Author | : Luca Domenico D’Andrea |
Publisher | : Frontiers Media SA |
Total Pages | : 135 |
Release | : 2021-12-06 |
Genre | : Science |
ISBN | : 2889718204 |
Author | : Lisa Ann Eidenschink |
Publisher | : |
Total Pages | : 180 |
Release | : 2009 |
Genre | : Peptides |
ISBN | : |
Author | : Ken Dill |
Publisher | : Garland Science |
Total Pages | : |
Release | : 2017-09-19 |
Genre | : Medical |
ISBN | : 1351815008 |
Protein Actions: Principles and Modeling is aimed at graduates, advanced undergraduates, and any professional who seeks an introduction to the biological, chemical, and physical properties of proteins. Broadly accessible to biophysicists and biochemists, it will be particularly useful to student and professional structural biologists and molecular biophysicists, bioinformaticians and computational biologists, biological chemists (particularly drug designers) and molecular bioengineers. The book begins by introducing the basic principles of protein structure and function. Some readers will be familiar with aspects of this, but the authors build up a more quantitative approach than their competitors. Emphasizing concepts and theory rather than experimental techniques, the book shows how proteins can be analyzed using the disciplines of elementary statistical mechanics, energetics, and kinetics. These chapters illuminate how proteins attain biologically active states and the properties of those states. The book ends with a synopsis the roles of computational biology and bioinformatics in protein science.
Author | : Dev Bukhsh Singh |
Publisher | : Springer Nature |
Total Pages | : 458 |
Release | : 2020-07-02 |
Genre | : Science |
ISBN | : 9811555303 |
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.
Author | : Jurriaan Huskens |
Publisher | : John Wiley & Sons |
Total Pages | : 434 |
Release | : 2018-02-05 |
Genre | : Science |
ISBN | : 1119143462 |
Connects fundamental knowledge of multivalent interactions with current practice and state-of-the-art applications Multivalency is a widespread phenomenon, with applications spanning supramolecular chemistry, materials chemistry, pharmaceutical chemistry and biochemistry. This advanced textbook provides students and junior scientists with an excellent introduction to the fundamentals of multivalent interactions, whilst expanding the knowledge of experienced researchers in the field. Multivalency: Concepts, Research & Applications is divided into three parts. Part one provides background knowledge on various aspects of multivalency and cooperativity and presents practical methods for their study. Fundamental aspects such as thermodynamics, kinetics and the principle of effective molarity are described, and characterisation methods, experimental methodologies and data treatment methods are also discussed. Parts two and three provide an overview of current systems in which multivalency plays an important role in chemistry and biology, with a focus on the design rules, underlying chemistry and the fundamental principles of multivalency. The systems covered range from chemical/materials-based ones such as dendrimers and sensors, to biological systems including cell recognition and protein binding. Examples and case studies from biochemistry/bioorganic chemistry as well as synthetic systems feature throughout the book. Introduces students and young scientists to the field of multivalent interactions and assists experienced researchers utilising the methodologies in their work Features examples and case studies from biochemistry/bioorganic chemistry, as well as synthetic systems throughout the book Edited by leading experts in the field with contributions from established scientists Multivalency: Concepts, Research & Applications is recommended for graduate students and junior scientists in supramolecular chemistry and related fields, looking for an introduction to multivalent interactions. It is also highly useful to experienced academics and scientists in industry working on research relating to multivalent and cooperative systems in supramolecular chemistry, organic chemistry, pharmaceutical chemistry, chemical biology, biochemistry, materials science and nanotechnology.
Author | : Tatiana Koshlan |
Publisher | : Springer |
Total Pages | : 367 |
Release | : 2018-08-24 |
Genre | : Science |
ISBN | : 3319983040 |
This book is devoted to the physical and mathematical modeling of the formation of complexes of protein molecules. The models developed show remarkable sensitivity to the amino acid sequences of proteins, which facilitates experimental studies and allows one to reduce the associated costs by reducing the number of measurements required according to the developed criteria. These models make it possible to reach a conclusion about the interactions between different amino acid chains and to identify more stable sites on proteins. The models also take the phosphorylation of amino acid residues into account. At the end of the book, the authors present possible directions of application of their physical and mathematical models in clinical medicine.
Author | : Wei Wang |
Publisher | : |
Total Pages | : 160 |
Release | : 2014 |
Genre | : Bioinformatics |
ISBN | : |
Protein-surface interactions, no matter structured or unstructured, are important in both biological and man-made systems. Unstructured interactions are more difficult to study with conventional techniques due to the lack of a specific binding structure. In this dissertation, a novel approach is employed to study the unstructured interactions between proteins and heterogonous surfaces, by looking at a large number of different binding partners at surfaces and using the binding information to understand the chemistry of binding. In this regard, surface-bound peptide arrays are used as a model for the study. Specifically, in Chapter 2, the effects of charge, hydrophobicity and length of surface-bound peptides on binding affinity for specific globular proteins (beta-galactosidase and alpha1-antitrypsin) and relative binding of different proteins were examined with LC Sciences peptide array platform. While the general charge and hydrophobicity of the peptides are certainly important, more surprising is that beta-galactosidase affinity for the surface does not simply increase with the length of the peptide. Another interesting observation that leads to the next part of the study is that even very short surface-bound peptides can have both strong and selective interactions with proteins. Hence, in Chapter 3, selected tetrapeptide sequences with known binding characteristics to beta-galactosidase are used as building blocks to create longer sequences to see if the binding function can be added together. The conclusion is that while adding two component sequences together can either greatly increase or decrease overall binding and specificity, the contribution to the binding affinity and specificity of the individual binding components is strongly dependent on their position in the peptide. Finally, in Chapter 4, another array platform is utilized to overcome the limitations associated with LC Sciences. It is found that effects of peptide sequence properties on IgG binding with HealthTell array are quiet similar to what was observed with beta-galactosidase on LC Science array surface. In summary, the approach presented in this dissertation can provide binding information for both structured and unstructured interactions taking place at complex surfaces and has the potential to help develop surfaces covered with specific short peptide sequences with relatively specific protein interaction profiles.