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Author: John E. Leffler
Publisher: Courier Corporation
Published: 1989-01-01
Total Pages: 500
ISBN-13: 9780486660684
DOWNLOAD EBOOKGraduate-level text stresses extrathermodynamic approach to quantitative prediction and constructs a logical framework that encompasses and classifies all known extrathermodynamic relationships. Numerous figures and tables. Author and Subject Indexes.
Author: Gabriel Waksman
Publisher: Springer Science & Business Media
Published: 2006-12-22
Total Pages: 325
ISBN-13: 0387245324
DOWNLOAD EBOOKGabriel 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.
Author: Y. Moroi
Publisher: Springer Science & Business Media
Published: 1992-03-31
Total Pages: 274
ISBN-13: 9780306439964
DOWNLOAD EBOOKAlmost thirty years ago the author began his studies in colloid chemistry at the laboratory of Professor Ryohei Matuura of Kyushu University. His graduate thesis was on the elimination of radioactive species from aqueous solution by foam fractionation. He has, except for a few years of absence, been at the university ever since, and many students have contributed to his subsequent work on micelle formation and related phenomena. Nearly sixty papers have been published thus far. Recently, in search of a new orientation, he decided to assemble his findings and publish them in book form for review and critique. In addition, his use of the mass action model of micelle has received much criticism, especially since the introduction of the phase separation model. Many recent reports have postulated a role for Laplace pressure in micellization. Although such a hypothesis would provide an easy explanation for micelle formation, it neglects the fact that an interfacial tension exists between two macroscopic phases. The present book cautions against too ready an acceptance of the phase separation model of micelle formation. Most references cited in this book are studies introduced in small group meetings of colloid chemists, the participants at which included Professors M. Saito, M. Manabe, S. Kaneshina, S. Miyagishi, A. Yamauchi, H. Akisada, H. Matuo, M. Sakai, and Drs. O. Shibata, N. Nishikido, and Y. Murata, to whom the author wishes to express his gratitude for useful discussions.
Author: Robert P H Gasser
Publisher: World Scientific Publishing Company
Published: 1995-09-26
Total Pages: 190
ISBN-13: 9813103132
DOWNLOAD EBOOKStatistical thermodynamics plays a vital linking role between quantum theory and chemical thermodynamics, yet students often find the subject unpalatable.In this updated version of a popular text, the authors overcome this by emphasising the concepts involved, in particular demystifying the partition function. They do not get bogged down in the mathematical niceties that are essential for a profound study of the subject but which can confuse the beginner. Strong emphasis is placed on the physical basis of statistical thermodynamics and the relations with experiment. After a clear exposition of the distribution laws, partition functions, heat capacities, chemical equilibria and kinetics, the subject is further illuminated by a discussion of low-temperature phenomena and spectroscopy. The coverage is brought right up to date with a chapter on computer simulation and a final section which ranges beyond the narrow limits usually associated with student texts to emphasise the common dependence of macroscopic behaviour on the properties of constituent atoms and molecules.Since first published in 1974 as ‘Entropy and Energy Levels’, the book has been very popular with students. This revised and updated version will no doubt serve the same needs.
Author: H. Gutfreund
Publisher: Cambridge University Press
Published: 1995-09-14
Total Pages: 364
ISBN-13: 9780521485869
DOWNLOAD EBOOKThe aim of the book is to introduce the reader to the kinetic analysis of a wide range of biological processes at the molecular level. It is intended to show that the same approach can be used to resolve the number of steps in enzyme reactions, muscle contraction, visual perception and ligand binding receptors that trigger other physiological processes. Attention is also given to methods for characterizing these steps in chemical terms. Although the treatment is mainly theoretical, a wide range of examples and experimental techniques are also introduced and an historical approach is used to demonstrate the development of the theory and experimental techniques of kinetic analysis in biology.
Author: Biman Bagchi
Publisher: Cambridge University Press
Published: 2013-11-14
Total Pages: 383
ISBN-13: 1107037298
DOWNLOAD EBOOKA unified overview of the dynamical properties of water and its unique and diverse role in biological and chemical processes.
Author: Holger Gohlke
Publisher: John Wiley & Sons
Published: 2012-05-21
Total Pages: 361
ISBN-13: 3527329668
DOWNLOAD EBOOKInnovative 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.
Author: Ingo Müller
Publisher: Springer Science & Business Media
Published: 2006-06-15
Total Pages: 268
ISBN-13: 3540323805
DOWNLOAD EBOOKIntroductory textbook introducing the concept of competition of entropy and energy with various examples. Thermodynamics textbook explaining the roles of entropy and energy as prime movers of nature.
Author: Roger Gregory
Publisher: CRC Press
Published: 2024-11-01
Total Pages: 596
ISBN-13: 1040282512
DOWNLOAD EBOOKThis work covers advances in the interactions of proteins with their solvent environment and provides fundamental physical information useful for the application of proteins in biotechnology and industrial processes. It discusses in detail structure, dynamic and thermodynamic aspects of protein hydration, as well as proteins in aqueous and organic solvents as they relate to protein function, stability and folding.
Author: György Keserü
Publisher: John Wiley & Sons
Published: 2015-08-17
Total Pages: 360
ISBN-13: 352733582X
DOWNLOAD EBOOKThis 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.
