高等学校化学学报 ›› 1992, Vol. 13 ›› Issue (9): 1271.

• 论文 • 上一篇    下一篇

蛋白质中氨基酸残基和肽片段间的特异识别研究

王玉宏1, 刘晓青1, 李惟1, 马速成2   

  1. 1. 吉林大学分子生物学系, 长春, 130023;
    2. 长春地质学院计算中心
  • 收稿日期:1991-10-28 出版日期:1992-09-24 发布日期:1992-09-24
  • 通讯作者: 李惟

Specific Recognition of Interresidue and interpeptide in Proteins

WANG Yu-Hong1, LIU Xiao-Qing1, LI Wei1, MA Su-Cheng2   

  1. 1. Department of Molecular Biology, Jilin University Changchun, 130023;
    2. Computational Centre, Changchun Geologrcal College
  • Received:1991-10-28 Online:1992-09-24 Published:1992-09-24

摘要: 本文从蛋白质晶体数据库中选取了125种非同源蛋白质,对其平行和反平行相互作用肽片段中残基间的亲和性进行了统计分析,得到了氨基酸残基和肽片段间的配对规律.本文所报道的残基间配对亲和性可用于蛋白质的折叠计算、结构预测和蛋白质工程实验设计中.

关键词: 疏水性, 残基配对, 肽片段, 特异识别

Abstract: We extracted 524 pairs of parallel peptide segments and 2283 pairs of anti-parallel pep-tide segments of 5 residues long from the 125 heterogeneous proteins,and then applied the statistical analysis algorithm to calculating residue-residue pairing frequencies.Finally the relative pairing frequencies or affinities were obtained.From the affinities it can be seen that there exists substantially specific residue-reside pairing between two strands of the interactive peptide segments.The obtained results will be helpful for protein engineering and structure prediction.

Key words: Hydrophobicity, Residue pairing, Peptide segment, Specific recognition

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