首页    期刊浏览 2024年12月06日 星期五
登录注册

文章基本信息

  • 标题:The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins
  • 本地全文:下载
  • 作者:Gerhard Hummer ; Shekhar Garde ; Angel E. García
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1998
  • 卷号:95
  • 期号:4
  • 页码:1552-1555
  • DOI:10.1073/pnas.95.4.1552
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Proteins can be denatured by pressures of a few hundred MPa. This finding apparently contradicts the most widely used model of protein stability, where the formation of a hydrophobic core drives protein folding. The pressure denaturation puzzle is resolved by focusing on the pressure-dependent transfer of water into the protein interior, in contrast to the transfer of nonpolar residues into water, the approach commonly taken in models of protein unfolding. Pressure denaturation of proteins can then be explained by the pressure destabilization of hydrophobic aggregates by using an information theory model of hydrophobic interactions. Pressure-denatured proteins, unlike heat-denatured proteins, retain a compact structure with water molecules penetrating their core. Activation volumes for hydrophobic contributions to protein folding and unfolding kinetics are positive. Clathrate hydrates are predicted to form by virtually the same mechanism that drives pressure denaturation of proteins.
  • 关键词:protein folding ; protein folding kinetics ; hydrophobic effect ; activation volumes ; protein unfolding
国家哲学社会科学文献中心版权所有