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by Arieh Ben-Naim

ePub Hydrophobic Interactions download
Arieh Ben-Naim
Springer; Softcover reprint of edition (January 31, 1980)
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Hydrophobic Interactions. Authors: Ben-Naim, Arieh. Temperature and Pressure Dependence of the Hydrophobic Interactions.

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Arieh Ben-Naim (Hebrew: אריה בן-נאים; Jerusalem, 11 July 1934) is a professor of physical chemistry who retired in 2003 from the Hebrew University of Jerusalem. He has made major contributions over 40 years to the theory of the structure of water, aqueous solutions and lic interactions. He is mainly concerned with theoretical and experimental aspects of the general theory of liquids and solutions.

A A. Ben Naim Entropy for smart kids and their curious parents, Cambridge . This book discusses entropy and the Second Law of Thermodynamic In such way that everyone can understand its subject matter.

Ben-Naim, Discover Probability; How to Use it, How to Avoid Misusing it and How it Affects Every Aspect of Your Life, World Scientific, Singapore (2014). A. Ben-Naim, Information, Entropy, Life and the Universe. What we know and what we do not know, World Scientific, Singapore (2015). Ben Naim Entropy for smart kids and their curious parents, Cambridge Scholar Publishing, (2019). Entropy is one of the must interesting concepts in physics.

We analyze all the contributions to the standard free energy of association between two proteins. We find that the solvent-induced interactions between two (or more) hydrophilic groups can turn a highly unfavorable process of association into a highly favorable one.

Arieh Ben-Naim (Author)

Arieh Ben-Naim (Author). Find all the books, read about the author, and more. Are you an author? Learn about Author Central. Arieh Ben-Naim (Author). This book 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. In Part I of this series, it was shown that the role of the so-called hydrophobic effect in biochemical processes was over-exaggerated.

AUTHORS: Arieh Ben-Naim. KEYWORDS: Protein Folding, Protein Association, Molecular Recognition, Hydrophobic, Hydrophilic Interactions. JOURNAL NAME: Open Journal of Biophysics, Vo. N., October 18, 2011. ABSTRACT: In the beginning everything was explained in Biochemistry in terms of hydrogen-bonds (HB). Then, the devastating blow, known as the HB-inventory argument came; hydrogen bonding with water molecules compete with intramolecular hydrogen-bonds. As a result, the HBs paradigm fell from grace.

Cite this paper: Arieh Ben-Naim. Inversion of the lic Paradigm Demystifies the Protein Folding and Self-Assembly of Problems. International Journal of Physics. doi: 1. 2691/ijp-1-3-2. Correspondence to: Arieh Ben-Naim, Department of Physical Chemistry The Hebrew University of Jerusalem, Jerusalem, Israel. The idea that the hydrophobic effect is the major driving force for processes such as protein folding and protein-protein association has prevailed in the biochemical literature for over half a century. This button opens a dialog that displays additional images for this product with the option to zoom in or out. Tell us if something is incorrect. Hydrophobic Interactions.

Arieh Ben-Naim is a modern antagonist of the term entropy. He advocates abandoning the word entropy altogether, and replacing it with missing information. He also indicates that the Kelvin temperature scale artificially introduces the units of thermodynamic entropy. Because this temperature scale was introduced before the atomic, microscopic nature of matter was widely accepted, the Boltzmann constant was necessary. S kBlog(W) could be expressed simply as S log(W) if the energy units for temperature kBT were used

My personal involvement with the problem of hydrophobic interactions (HI) began about ten years ago. At that time I was asked to write a review article on the properties of aqueous solutions of nonpolar solutes. While surveying the literature on this subject I found numerous discussions of the concept of HI. My interest in these interactions increased especially after reading the now classical review of W. Kauzmann (1959), in which the importance of the HI to biochemical processes is stressed. Yet, in spite of having read quite extensively on the various aspects of the subject, I acquired only a very vague idea of what people actually had in mind when referring to HI. In fact, it became quite clear that the term HI was applied by different authors to describe and interpret quite different phenomena occurring in aqueous solutions. Thus, even the most fundamental question of the very definition of the concept of HI remained unanswered. But other questions followed, e. g. : Are HI really a well­ established experimental fact? Is there any relation between HI and the peculiar properties of water? Is the phenomenon really unique to aqueous solutions? Finally, perhaps the most crucial question I sought to answer was whether or not there exists hard evidence that HI are really important -as often claimed-in biological processes.