Unknown

Dataset Information

0

Segmental Deuteration of α-Synuclein for Neutron Reflectometry on Tethered Bilayers.


ABSTRACT: Neutron reflectometry (NR) is uniquely suited for studying protein interaction with phospholipid bilayers along the bilayer normal on an angstrom scale. However, NR on its own cannot discern specific membrane-bound regions due to a lack of scattering contrast within a protein. Here we report the successful coupling of native chemical ligation (NCL) and NR to study α-synuclein (α-syn), a membrane-binding neuronal protein central in Parkinson's disease. Two α-syn variants were generated where either the first 86 or last 54 residues are deuterated, allowing for region-specific contrast within the protein and the identification of membrane interacting residues by NR. Residues 1-86 are positioned at the hydrocarbon/headgroup interface of the outer leaflet, whereas the density distribution of the 54 C-terminal residues ranges from the hydrocarbon region to the aqueous environment. Coupling of NCL and NR should have broad utility in studies of membrane protein folding.

SUBMITTER: Jiang Z 

PROVIDER: S-EPMC5367044 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

Segmental Deuteration of α-Synuclein for Neutron Reflectometry on Tethered Bilayers.

Jiang Zhiping Z   Heinrich Frank F   McGlinchey Ryan P RP   Gruschus James M JM   Lee Jennifer C JC  

The journal of physical chemistry letters 20161209 1


Neutron reflectometry (NR) is uniquely suited for studying protein interaction with phospholipid bilayers along the bilayer normal on an angstrom scale. However, NR on its own cannot discern specific membrane-bound regions due to a lack of scattering contrast within a protein. Here we report the successful coupling of native chemical ligation (NCL) and NR to study α-synuclein (α-syn), a membrane-binding neuronal protein central in Parkinson's disease. Two α-syn variants were generated where eith  ...[more]

Similar Datasets

| S-EPMC4295019 | biostudies-literature
| S-EPMC10079580 | biostudies-literature
| S-EPMC3274814 | biostudies-other
| S-EPMC9348865 | biostudies-literature
| S-EPMC8933405 | biostudies-literature
| S-EPMC6661114 | biostudies-literature
| S-EPMC3098118 | biostudies-literature
| S-EPMC4838215 | biostudies-literature
| S-EPMC7710489 | biostudies-literature
| S-EPMC4070068 | biostudies-literature