Journal article

The alpha-M1 segment of the nicotinic acetylcholine receptor exhibits conformational flexibility in a membrane environment

MRR de Planque, DTS Rijkers, JI Fletcher, RMJ Liskamp, F Separovic

Biochimica et Biophysica Acta-Biomembranes | ELSEVIER SCIENCE BV | Published : 2004

DOI: 10.1016/j.bbamem.2004.06.021

University of Melbourne Researchers

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Keywords

Science & Technology
Infrared-Spectroscopy
Secondary Structure
Biochemistry & Molecular Biology
Chemical-Shifts
Liposomes
Protein Structure, Tertiary
Binding-Sites
Nuclear Magnetic Resonance, Biomolecular
Conformation
Proline
Animals
Isotopes
Pliability
Model Membranes
Biophysics
Circular-Dichroism Spectra
Helical Peptides
Exchange-Resistant Core
Peptide Fragments
Phosphatidylcholine Model Membranes
Motion
Protein Structure, Secondary
Alpha M1 Transmembrane Segment
Spatial Structure
Nicotinic Acetylcholine Receptor
Phosphatidylcholines
Solid-State Nmr
M4 Transmembrane Domain
Life Sciences & Biomedicine
Receptors, Nicotinic
Membrane Proteins
Torpedo
Amino Acid Sequence