title: Folding of the C-terminal fragment V111-D143 of staphylococcal nuclease in aqueous solution.
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.
authors.affiliation: National Laboratory of Biomacromolecules, Center for Structural and Molecular Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing, PR China.
authors.forename: Yong
authors.initials: Y
authors.lastname: Geng
authors.forename: Min
authors.initials: M
authors.lastname: Wang
authors.forename: Tao
authors.initials: T
authors.lastname: Xie
authors.forename: Yingang
authors.initials: Y
authors.lastname: Feng
authors.forename: Jinfeng
authors.initials: J
authors.lastname: Wang
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D004578:Electron Spin Resonance Spectroscopy; D008836:Micrococcal Nuclease / Q000737:chemistry*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D010446:Peptide Fragments; D008836:Micrococcal Nuclease