Fourier transform coupled tryptophan scanning mutagenesis identifies a bending point on the lipid-exposed δM3 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor.
about
Assessment of the functionality and stability of detergent purified nAChR from Torpedo using lipidic matrixes and macroscopic electrophysiology.Tryptophan scanning mutagenesis reveals distortions in the helical structure of the δM4 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor.
P2860
Fourier transform coupled tryptophan scanning mutagenesis identifies a bending point on the lipid-exposed δM3 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor.
description
2011 nî lūn-bûn
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name
Fourier transform coupled tryp ...... otinic acetylcholine receptor.
@en
Fourier transform coupled tryp ...... otinic acetylcholine receptor.
@nl
type
label
Fourier transform coupled tryp ...... otinic acetylcholine receptor.
@en
Fourier transform coupled tryp ...... otinic acetylcholine receptor.
@nl
prefLabel
Fourier transform coupled tryp ...... otinic acetylcholine receptor.
@en
Fourier transform coupled tryp ...... otinic acetylcholine receptor.
@nl
P2093
P2860
P356
P1433
P1476
Fourier transform coupled tryp ...... otinic acetylcholine receptor.
@en
P2093
Daniel Caballero-Rivera
David A Torres-Núñez
Jessica Oyola-Cintrón
Jose D Otero-Cruz
José A Lasalde-Dominicci
Omar A Cruz-Nieves
P2860
P304
P356
10.4161/CHAN.5.4.17082
P577
2011-07-01T00:00:00Z