The role of tryptophan in staphylococcal nuclease stability

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题名:	The role of tryptophan in staphylococcal nuclease stability
作者:	Hu,HY;Wu,MC;Fang,HJ;Forrest,MD;Hu,CK;Tsong,TY;Chen,HM
贡献者:	物理學系
关键词:	SITE-DIRECTED MUTAGENESIS;MOLTEN GLOBULE STATE;RESIDUAL STRUCTURE;PROTEIN;CONFORMATION;FRAGMENTS;COMPACT;MUTANT;MODEL;NMR
日期:	2010
上传时间:	2012-06-11 10:47:14 (UTC+8)
出版者:	國立中央大學
摘要:	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. (C) 2010 Elsevier B.V. All rights reserved.
關聯:	BIOPHYSICAL CHEMISTRY
显示于类别:	[物理學系] 期刊論文

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