Molecular Theory Of Water And Aqueous Solutions - Part Ii: The Role Of Water In Protein Folding, Self-Assembly And Molecular Recognition, Ben-Naim Arieh
Описание: Starts out by presenting the evidence for hydrophilic interactions in biochemical processes and then goes on to describe the applications of the hydrophilic interactions in these processes, specifically protein folding, protein association, self assembly and molecular recognition.
This book reviews current research on the important processes involved in neurodegenerative diseases (e.g. Alzheimer's disease) and the peptides and proteins involved in the amyloidogenic processes. It covers the design and developments of anti-amyloid inhibitors, and gives readers a fundamental understanding of the underlying oligomerization and aggregation processes of these diseases from both computational and experimental points of view.
Описание: The second volume continues to fill the gap in protein review and protocal literature while summarizing recent achievements in the understanding of the relationships between protein misfoldings, aggregation, and development of protein deposition disorders. The focus of Part B is the molecular basis of differential disorders.
Описание: This unique volume reviews the beautiful architectures and varying mechanical actions of the set of specialized cellular proteins called molecular chaperones, which provide essential kinetic assistance to processes of protein folding and unfolding in the cell.
Автор: Ben-Naim Arieh Название: Protein Folding Problem And Its Solutions, The ISBN: 9814436356 ISBN-13(EAN): 9789814436359 Издательство: World Scientific Publishing Рейтинг: Цена: 15840.00 р. Наличие на складе: Есть у поставщика Поставка под заказ.
Описание: This book presents a new approach to the Protein Folding Problem. It starts with a clear description of what the protein folding problem involves. Then, it suggests non-conventional answers to some of the questions posed. In particular, it emphasizes the importance of hydrophilic interactions and hydrophilic forces, rather than the hydrophobic effects, for the stability of the native structure of proteins, as well for the speed of the folding process.
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