% IMPORTANT: The following is UTF-8 encoded. This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.
@ARTICLE{Scheidt:59162,
author = {Scheidt, H. A. and Vogel, A. and Eckhoff, A. and Koenig, B.
W. and Huster, D.},
title = {{S}olid-state {NMR} characterization of the putative
membrane anchor of {TWD}1 from {A}rabidopsis thaliana},
journal = {European biophysics journal},
volume = {36},
issn = {0175-7571},
address = {Berlin},
publisher = {Springer},
reportid = {PreJuSER-59162},
year = {2007},
note = {Record converted from VDB: 12.11.2012},
abstract = {Structure and membrane interaction of a 31 amino acid
residue fragment of the membrane bound FKBP-like protein
twisted dwarf 1 (TWD1) from Arabidopsis thaliana was
investigated by solid-state NMR spectroscopy. The studied
peptide TWD1(335-365) contained the putative membrane anchor
of the protein (residues 339-357) that was previously
predicted by sequence hydrophobicity analysis. The TWD1
peptide was synthesized by standard solid phase peptide
synthesis and contained three uniformly (13)C- and
(15)N-labelled residues (Phe 340, Val 350, Ala 364). The
peptide was incorporated into either multilamellar vesicles
or oriented planar membranes composed of an equimolar
ternary phospholipid mixture (POPC, POPE, POPG), where the
POPC was sn-1 chain-deuterated. (31)P NMR spectra of the
membrane in the absence and in the presence of the peptide
showed axially symmetric powder patterns indicative of a
lamellar bilayer phase. Further, the addition of peptide
caused a decrease in the lipid hydrocarbon chain order as
indicated by reduced quadrupolar splittings in the (2)H NMR
spectra of the POPC in the membrane. The conformation of
TWD1(335-365) was investigated by (13)C cross-polarization
magic-angle spinning NMR spectroscopy. At a temperature of
-30 degrees C all peptide signals were resolved and could be
fully assigned in two-dimensional proton-driven (13)C spin
diffusion and (13)C single quantum/double quantum
correlation experiments. The isotropic chemical shift values
for Phe 340 and Val 350 exhibited the signature of a regular
alpha-helix. Chemical shifts typical for a random coil
conformation were observed for Ala 364 located close to the
C-terminus of the peptide. Static (15)N NMR spectra of
TWD1(335-365) in mechanically aligned lipid bilayers
demonstrated that the helical segment of TWD1(335-365)
adopts an orientation perpendicular to the membrane normal.
At 30 degrees C, the peptide undergoes intermediate time
scale motions.},
keywords = {Arabidopsis Proteins: chemistry / Binding Sites / Cell
Membrane: chemistry / Glycosylphosphatidylinositols:
chemistry / Lipid Bilayers: chemistry / Magnetic Resonance
Spectroscopy / Membrane Fusion / Protein Binding /
Tacrolimus Binding Proteins: chemistry / Arabidopsis
Proteins (NLM Chemicals) / Glycosylphosphatidylinositols
(NLM Chemicals) / Lipid Bilayers (NLM Chemicals) / TWD1
protein, Arabidopsis (NLM Chemicals) / Tacrolimus Binding
Proteins (NLM Chemicals) / J (WoSType)},
cin = {INB-2},
ddc = {570},
cid = {I:(DE-Juel1)VDB805},
pnm = {Funktion und Dysfunktion des Nervensystems},
pid = {G:(DE-Juel1)FUEK409},
shelfmark = {Biophysics},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:17033777},
UT = {WOS:000245826200014},
doi = {10.1007/s00249-006-0094-2},
url = {https://juser.fz-juelich.de/record/59162},
}