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

• DOI: 10.2174/092986607781483769
• Publication Date: 2007-08-09T23:54:36Z
• Authors: Yong Geng; Min Wang; Tao Xie; Yingang Feng; Jinfeng Wang
• Keywords: Protein Folding; 0303 health sciences; 03 medical and health sciences; Protein Conformation; Circular Dichroism; Molecular Sequence Data; Electron Spin Resonance Spectroscopy; Micrococcal Nuclease; Amino Acid Sequence; Nuclear Magnetic Resonance, Biomolecular; Peptide Fragments

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.