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Download Protein Interactions djvu

Download Protein Interactions djvu

by G. Weber

Author: G. Weber
Subcategory: Medicine & Health Sciences
Language: English
Publisher: Springer; 1992 edition (May 31, 1992)
Pages: 294 pages
Category: Other
Rating: 4.7
Other formats: doc lit docx rtf

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Protein Interactions has been added to your Cart. The theoretical framework is elementary enough to be appreciated by beginning graduate students in the biological sciences: this would make an excellent textbook for advanced courses. the reader is bound to come away with a better understanding of. protein systems. I highly recommend this book to all who study proteins.

Protein Interactions. Hardcover 229,00 €. price for Russian Federation (gross).

Protein Interactions book. This book presents a detailed examination of the physical properties. ISBN13:9780412030314.

Find nearly any book by G. Weber. Get the best deal by comparing prices from over 100,000 booksellers. Residential Treatment of Emotionally Disturbed Children.

Protein interactions, which include interactions between proteins and other biomolecules, are essential to all .

Protein interactions, which include interactions between proteins and other biomolecules, are essential to all aspects of biological processes, such as cell growth, differentiation, and apoptosis. Therefore, investigation and modulation of protein interactions are of significance as it not only reveals the mechanism governing cellular activity, but also leads to potential agents for the treatment of various diseases.

Protein–protein interactions (PPIs) are the physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by electrostatic forces including the hydrophobic effect. Many are physical contacts with molecular associations between chains that occur in a cell or in a living organism in a specific biomolecular context.

As an indifferent osmolyte urea should promote the stability of the protein aggregates under pressure, and the decrease in pressure stability with urea concentration demonstrates that such indirect solvent effects are not significant for this case, and that the progressive destabilization is the result of direct protein-urea interactions.

Эту книгу можно прочитать в Google Play Книгах на компьютере, а также на устройствах Android и iO.

Эту книгу можно прочитать в Google Play Книгах на компьютере, а также на устройствах Android и iOS. Выделяйте текст, добавляйте закладки и делайте заметки, скачав книгу "Proteomics and Protein-Protein Interactions: Biology, Chemistry, Bioinformatics, and Drug Design" для чтения в офлайн-режиме. 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.

Weber, G. (1992) Protein Interactions. Chapman and Hall, New York. Note: A book containing 16 chapters all written by G. 179. Weber, G. (1991) Functional significance of the free volume inside proteins: A conjecture

Weber, G. (1991) Functional significance of the free volume inside proteins: A conjecture. Lu . X and Zhang . S. World Scientific, Hong-Kong and London, pp. 221-225.

This book presents a detailed examination of the physical properties of proteins and their associations with solvents, ligands, and each other. Incorporating observations from his classic work on the thermodynamics of protein-protein and protein-ligand interactions, the internationally recognized author offers a complete conceptual and quantitative description of proteins and their associations. The book begins with an overview of basic thermodynamic principles and goes on to describe the covalent and noncovalent binding of single and multiple ligands and their effects on protein-protein associations. Discussions of protein-solvent interactions address issues including protein folding, membrane associations, and protein dynamics. Attention is given to the effect of temperature and pressure on protein structure, oligomerization, and ligand binding, as well as to ideas about the basis of biological specificity. Although experimental work is discussed throughout the text, the book is not technique oriented. Its theoretical framework is clear, general and easily understandable, making this an essential textbook for beginning graduate students in biological sciences, as well as a valuable reference for advanced researchers in industry and academia.