﻿<?xml version="1.0" encoding="UTF-8"?>
<records>
  <record>
    <language>eng</language>
    <publisher>Science and Education Publishing</publisher>
    <journalTitle>International Journal of Physics</journalTitle>
    <publicationDate>2013-05-08</publicationDate>
    <volume>1</volume>
    <issue>1</issue>
    <startPage>66</startPage>
    <endPage>71</endPage>
    <doi>10.12691/ijp-1-3-2</doi>
    <publisherRecordId>IJP2013132</publisherRecordId>
    <documentType>article</documentType>
    <title language="eng">Inversion of the Hydrophobic/Hydrophilic Paradigm Demystifies the Protein Folding and Self-Assembly of Problems</title>
    <authors>
      <author>
        <name>Arieh Ben-Naim</name>
        <email>arieh@fh.huji.ac.il</email>
        <affiliationId>1</affiliationId>
      </author>
    </authors>
    <affiliationsList>
      <affiliationName affiliationId="1">Department of Physical Chemistry The Hebrew University of Jerusalem, Jerusalem, Israel</affiliationName>
    </affiliationsList>
    <abstract language="eng">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. It has recently become clear that the evidence in favor of the hydrophobic paradigm has totally dissipated. The dominance of the hydrophobic effect has been reduced into nothing but a myth. On the other hand, the new paradigm based on a host of hydrophilic effects has emerged. This new paradigm offers simple and straightforward answers to the long sought problems of protein folding and protein-protein association.</abstract>
    <fullTextUrl format="pdf">http://pubs.sciepub.com/ijp/1/3/2/ijp-1-3-2.pdf</fullTextUrl>
    <keywords language="eng">
      <keyword>
        <b>
        </b>proteins</keyword>
      <keyword>hydrophobic</keyword>
      <keyword>hydrophilic</keyword>
      <keyword>solvation</keyword>
      <keyword>folding</keyword>
      <keyword>association</keyword>
    </keywords>
  </record>
</records>