Folding of the C-Terminal Fragment V111-D143 of Staphylococcal Nuclease in Aqueous Solution

Title: Folding of the C-Terminal Fragment V111-D143 of Staphylococcal Nuclease in Aqueous Solution

Volume: 14 Issue: 8

Author(s): Yong Geng, Min Wang, Tao Xie, Yingang Feng and Jinfeng Wang

Affiliation:

Keywords: SNase(111-143), fragment, C-terminal sub-domain, helix-forming tendency, ensemble of interconverting conformations

Abstract: Studies of conformational features of fragments SNase(111-143) and SNase(118-143) and segment E122-K136 in 1-139 fragment (SNase139) suggest that the high intrinsic helical propensity can drive segment E122-K136 fold into a stable helix only when the segments V111-H121 and L137-D143 flanked on segment E122-K136 in staphylococcal nuclease (SNase) have stable folding.

Cite this article as:

Yong Geng , Min Wang , Tao Xie , Yingang Feng and Jinfeng Wang , Folding of the C-Terminal Fragment V111-D143 of Staphylococcal Nuclease in Aqueous Solution, Protein & Peptide Letters 2007; 14 (8) . https://dx.doi.org/10.2174/092986607781483769

DOI https://dx.doi.org/10.2174/092986607781483769	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305