Predicted secondary and tertiary structures of carp γ-crystallins with high methionine content: Role of methionine residues in the protein stability

Yen Chywan Liaw, Shyh Horng Chiou, Tschining Chang, Wen Chang Chang

研究成果: 雜誌貢獻文章同行評審

10 引文 斯高帕斯(Scopus)

摘要

A systematic structural comparison of several carp γ-crystalline with high methionine contents was made by the secondary-structure prediction together with computer model-building based on the established X-ray structure of calf γ-II crystallin. The overall surface hydrophilicity profile and the distribution of helices, β-sheets, and β-turns along the polypeptide chains are very similar among these carp γ-crystallins. In addition, their general polypeptide packing is close to the characteristic 2 domain/4 motif Greek key three-dimensional conformation depicted for the calf γ-II crystallin. Interestingly, most hydrophobic methionine residues are located on the protein surface with only a few buried inside the protein surface or in the interface between two motifs of each domain. The exposed hydrophobic and polarizable methionine cluster on the protein surface may have a bearing on the crystallin stability and dense packing in the piscine species, and probably also provides a malleable nonpolar surface for the interaction with other crystallin components for the maintenance of a clear and transparent lens.
原文英語
頁(從 - 到)341-344
頁數4
期刊Journal of Biochemistry
112
發行號3
DOIs
出版狀態已發佈 - 一月 1 1992
對外發佈

ASJC Scopus subject areas

  • 生物化學
  • 分子生物學

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