Distance-constraint approach to higher-order structures of globular proteins with empirically determined distances between amino acid residues

Hiroshi Wako, Yasushi Kubota

研究成果: Article

6 引用 (Scopus)

抜粋

An analysis of higher-order structures of globular proteins by means of a distance-constraint approach is presented. Conformations are generated for each of 21 test proteins of small and medium sizes by optimizing an objective function f=ΣΣwij(dij-〈dij〉)2, where dij is a distance between residues i and j in a calculated conformation, 〈dij〉 is an assigned distance to the (ij) pair of residues which is determined based on the statistics of known three-dimensional structures of 14 proteins in the earlier study, and wij is a weighting factor. 〈dij〉 involves information about hydrophobicity and hydrophilicity of each amino acid residue and about connectivity of a polypeptide chain. In these calculations, only the amino acid sequence is used as input data specific to a calculated protein. With respect to higher-order structures regenerated in the optimized conformations, the following properties are analyzed: (a) N14 of a residue, defined as the number of residues surrounding the residue located within a sphere of radius of 14 Å; (b) root-mean-square differences of the global and local conformations from the corresponding X-ray conformations; (c) distance profiles in the short and medium ranges; and (d) distance maps. The effects of supplementary information about locations of secondary structures and disulfide bonds are also examined to discuss the potential ability of this methodology to predict the three-dimensional structures of globular proteins.

元の言語English
ページ(範囲)233-243
ページ数11
ジャーナルJournal of Protein Chemistry
10
発行部数2
DOI
出版物ステータスPublished - 1991 4 1

ASJC Scopus subject areas

  • Biochemistry

フィンガープリント Distance-constraint approach to higher-order structures of globular proteins with empirically determined distances between amino acid residues' の研究トピックを掘り下げます。これらはともに一意のフィンガープリントを構成します。

  • これを引用