Myths And Verities In Protein Folding Theories, Ben-Naim Arieh
Автор: Ben-Naim Arieh Название: Myths And Verities In Protein Folding Theories ISBN: 9814725986 ISBN-13(EAN): 9789814725989 Издательство: World Scientific Publishing Рейтинг: Цена: 8870.00 р. Наличие на складе: Есть у поставщика Поставка под заказ.
Описание:
This book tells the story of a whole field of research which went disastrously wrong in many different directions when the wrong tools were used and the wrong targets aimed at, to solve a problem.
It all started from the misinterpretation of Schellman's experiments which were carried out in the mid-1950s, and which were later encapsulated by the so-called "Hydrogen-bond inventory argument." As a result, hydrogen bonding was ignored in protein folding; along with that a whole repertoire of other possible hydrophilic effects were not even considered. Against this background the hydrophobic effects, as suggested by Kauzmann, became the single most important effects in protein folding.
In addition, as a result of the misinterpretation of Anfinsen's hypothesis, as well as misunderstanding of the Second Law, people made futile attempts to search for the structure of proteins in the global minimum of either the Energy, or the Gibbs Energy Landscape.
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.
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.
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.
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