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    Please use this identifier to cite or link to this item: http://ir.lib.ncu.edu.tw/handle/987654321/52854


    Title: The role of tryptophan in staphylococcal nuclease stability
    Authors: Hu,HY;Wu,MC;Fang,HJ;Forrest,MD;Hu,CK;Tsong,TY;Chen,HM
    Contributors: 物理學系
    Keywords: SITE-DIRECTED MUTAGENESIS;MOLTEN GLOBULE STATE;RESIDUAL STRUCTURE;PROTEIN;CONFORMATION;FRAGMENTS;COMPACT;MUTANT;MODEL;NMR
    Date: 2010
    Issue Date: 2012-06-11 10:47:14 (UTC+8)
    Publisher: 國立中央大學
    Abstract: 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.
    Relation: BIOPHYSICAL CHEMISTRY
    Appears in Collections:[物理學系] 期刊論文

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