期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 107, 期 19, 页码 8623-8626出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1001299107
关键词
proteomics; sequence analysis
资金
- National Library of Medicine of the National Institutes of Health [LM06789]
Computational studies of the relationships between protein sequence, structure, and folding have traditionally relied on purely local sequence representations. Here we show that global representations, on the basis of parameters that encode information about complete sequences, contain otherwise inaccessible information about the organization of sequences. By studying the spectral properties of these parameters, we demonstrate that amino acid physical properties fall into two distinct classes. One class is comprised of properties that favor sequentially localized interaction clusters. The other class is comprised of properties that favor globally distributed interactions. This observation provides a bridge between two classic models of protein folding-the collapse model and the nucleation model-and provides a basis for understanding how any degree of intermediacy between these two extremes can occur.
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