Folding of the C-Terminal Fragment V111-D143 of Staphylococcal Nuclease in Aqueous Solution
Authors: Yong Geng; Min Wang; Tao Xie; Yingang Feng; Jinfeng Wang
Source: Protein and Peptide Letters, Volume 14, Number 8, August 2007 , pp. 747-755(9)
Publisher: Bentham Science Publishers
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.
Document Type: Research Article
Publication date: 2007-08-01
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.