期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 59, 期 5, 页码 859-869出版社
BIRKHAUSER VERLAG AG
DOI: 10.1007/s00018-002-8473-z
关键词
De novo design; template-assembled synthetic protein (TASP); carboprotein; 4-alpha-helix bundle; chemical synthesis; carbohydrate template; chemoselective ligation; peptide aldehyde
An understanding of very complex natural systems can often only be achieved through detailed studies of systems with a reduced complexity. Thus, de novo design of proteins allows the study of fundamental forces determining protein folding and stability, as well as protein-protein interactions, by analyses of protein models of structural motifs. In addition, de novo design may lead to new biomimetic molecules with novel properties. In a synthetic approach to achieve structural economy, rigid templates, sometimes called topological scaffolds, have been used to connect secondary-structure elements, most notably a-helices. By positioning the helices on the template, the unfavorable entropy of protein folding is reduced. In a novel class of chimeric molecules called carboproteins, carbohydrates are used as templates for de novo design of protein models. Recently, a strategy relying on chemoselective ligation of C-terminal peptide aldehydes to tetra-aminooxy functionalized monosaccharides has provided 7-kDa 4-alpha-helix bundle carboproteins.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据