The role of tryptophan in staphylococcal nuclease stability

Hong Yu Hu, Ming Chya Wu, Huey Jen Fang, Michael D. Forrest, Chin Kun Hu, Tian Yow Tsong, Hueih Min Chen

研究成果: 雜誌貢獻期刊論文同行評審

9 引文 斯高帕斯(Scopus)


Staphylococcal nuclease (SNase) has a single Trp residue at position 140. Circular dichroism, intrinsic and ANS-binding fluorescence, chemical titrations and enzymatic assays were used to measure the changes of its structure, stability and activities as the Trp was mutated or replaced to other positions. The results show that W140 is critical to SNase structure, stability, and function. Mutants such as W140A, F61W/W140A, and Y93W/W140A have unfolding, corrupted secondary and tertiary structures, diminished structural stability and attenuated catalytic activity as compared to the wild type. The deleterious effects of W140 substitution cannot be compensated by concurrent changes at topographical locations of position 61 or 93. Local hydrophobicity defined as a sum of hydrophobicity around a given residue within a distance is found to be a relevant property to SNase folding and stability.

頁(從 - 到)170-177
期刊Biophysical Chemistry
出版狀態已出版 - 10月 2010


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