Folding of the C-terminal fragment V111-D143 of staphylococcal nuclease in aqueous solution

Yong Geng; Min Wang; Tao Xie; Yingang Feng; Jinfeng Wang

doi:10.2174/092986607781483769

Folding of the C-terminal fragment V111-D143 of staphylococcal nuclease in aqueous solution

Protein Pept Lett. 2007;14(8):747-55. doi: 10.2174/092986607781483769.

Authors

Yong Geng¹, Min Wang, Tao Xie, Yingang Feng, Jinfeng Wang

Affiliation

¹ National Laboratory of Biomacromolecules, Center for Structural and Molecular Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing, PR China.

PMID: 17979813
DOI: 10.2174/092986607781483769

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Circular Dichroism
Electron Spin Resonance Spectroscopy
Micrococcal Nuclease / chemistry*
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
Peptide Fragments / chemistry
Protein Conformation
Protein Folding*

Substances

Peptide Fragments
Micrococcal Nuclease