NMR Study on Solution Configuration of
mHCN1 Pore Peptide
SUI
Tao, YU Han-Gang1, HU Hong-Yu2, SHI Yan-Hong, SONG Guo-Qiang*
( Institute of
Materia Medica, Shanghai Institutes for Biological Sciences, the Chinese Academy
of Sciences, Shanghai 200031, China;
1New York College of Osteopathic Medicine of New York Institute
of Technol ogy USA; 2Institute of Biochemistry and Cell Biology,
Shanghai Institutes for Biolo gical Sciences, the Chinese Academy of Sciences,
Shanghai 200031, China
)
Abstract
Spin systems for amino acid residues in mHZH1 pore region peptide have been identified
through analysis of 2D NMR spectra. The sequence-specific assignment of spin systems was obtained by
NOEs correlation in WET-NOESY spectra, and the complete assignment of proton resonances for backbone
and side chain has been achieved. ZHS software was used to calculate the structure of mHZH1 19 aa
peptide. The results show that an α-helix from residue 10 to residue 13 is formed within the
pore region. The results of NMR study on mHZH1 pore peptide provide the basis for further understanding
the mechanism of ion selectivity of channels.
Key
words mHCN1 pore peptide; NMR; solution structure
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