| Autor: |
Pashkov VS; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia., Maslennikov IV, Tchikin LD, Efremov RG, Ivanov VT, Arseniev AS |
| Jazyk: |
angličtina |
| Zdroj: |
FEBS letters [FEBS Lett] 1999 Aug 20; Vol. 457 (1), pp. 117-21. |
| DOI: |
10.1016/s0014-5793(99)01023-6 |
| Abstrakt: |
A synthetic peptide corresponding to the transmembrane segment M2 (residues 236-267) of the alpha-subunit of the nicotinic acetylcholine receptor from Torpedo californica has been studied by two dimensional 1H-NMR spectroscopy in a chloroform-methanol (1:1) mixture containing 0.1 M LiClO4. Reconstruction of the spatial structure of M2 from the NMR data resulted in an alpha-helix formed by residues 241-263. Distribution of the molecular hydrophobicity potential on the helix surface is very similar to that in five-helix bundles of proteins with a known three dimensional structure: two hydrophilic bands located on the opposite helix sides separated by strong hydrophobic zones. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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