首页    期刊浏览 2024年11月07日 星期四
登录注册

文章基本信息

  • 标题:Stereoelectronic and steric effects in side chains preorganize a protein main chain
  • 本地全文:下载
  • 作者:Matthew D. Shoulders ; Kenneth A. Satyshur ; Katrina T. Forest
  • 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:2010
  • 卷号:107
  • 期号:2
  • 页码:559-564
  • DOI:10.1073/pnas.0909592107
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Preorganization is shown to endow a protein with extraordinary conformational stability. This preorganization is achieved by installing side-chain substituents that impose stereoelectronic and steric effects that restrict main-chain torsion angles. Replacing proline residues in (ProProGly)7 collagen strands with 4-fluoroproline and 4-methylproline leads to the most stable known triple helices, having Tm values that are increased by > 50 {degrees}C. Differential scanning calorimetry data indicate an entropic basis to the hyperstability, as expected from an origin in preorganization. Structural data at a resolution of 1.21 A reveal a prototypical triple helix with insignificant deviations to its main chain, even though 2/3 of the residues are nonnatural. Thus, preorganization of a main chain by subtle changes to side chains can confer extraordinary conformational stability upon a protein without perturbing its structure.
  • 关键词:collagen triple helix ; nonnatural amino acid ; preorganization ; protein stability ; x-ray crystallography
国家哲学社会科学文献中心版权所有