球状蛋白质中序列与构象相关代码的分析。基于残基内信息构建立体化学字母表。

Analysis of the code relating sequence to conformation in globular proteins. Development of a stereochemical alphabet on the basis of intra-residue information.

Robson B, Pain R H

Biochem J. 1974 Sep;141(3):869-82. doi: 10.1042/bj1410869.

Abstract

The relation of primary sequence to all residue backbone conformations was explored to test out starting conformations for protein folding. 2. Information theory was used to obtain measures of information which quantitate the role of each residue in determining its own conformation; i.e. intra-residue information. 3. The information measures are plotted as a function of varphi, psi peptide-backbone angles and varphi, psi contour maps obtained for each of the 20 amino acids. These show characteristic differences between residues. 4. To find practical ways of relating sequence to varphi, psi angles, several types of stereochemical alphabet were investigated. The value of these was tested by using them to predict the varphi, psi angles of nine different proteins. 5. A difference plot was constructed to show regions of the sequence that require little or no information extra to the intra-residue information in order to predict a correct conformation. These regions are suggested to be candidates for nucleating sites in the protein.

摘要

研究了一级序列与所有残基主链构象的关系，以测试蛋白质折叠的起始构象。2. 利用信息论获得信息度量，这些度量量化了每个残基在确定自身构象中的作用，即残基内信息。3. 将信息度量作为φ、ψ肽主链角的函数绘制，并为20种氨基酸中的每一种获得φ、ψ等高线图。这些图显示了残基之间的特征差异。4. 为了找到将序列与φ、ψ角相关联的实用方法，研究了几种类型的立体化学字母表。通过用它们预测九种不同蛋白质的φ、ψ角来测试其价值。5. 构建了一个差异图，以显示序列中那些为了预测正确构象而除残基内信息外几乎不需要或不需要额外信息的区域。这些区域被认为是蛋白质中成核位点的候选区域。