NMR methods for studying the structure and dynamics of oncogenic and antihistaminic peptides in biomembranes.
We present several applications of both wide-line and magic angle spinning (MAS) solid-state NMR of bicelles in which are embedded fragments of a tyrosine kinase receptor or enkephalins. The magnetically orientable bicelle membranes are shown to be of particular interest for studying the functional properties of lipids and proteins in a state that is very close to their natural environment. Quadrupolar, dipolar and chemical shielding interactions can be used to determine minute alterations of internal membrane dynamics and the orientation of peptides with respect to the membrane plane. MAS of bicelles can in turn lead to high-resolution proton spectra of hydrated membranes. Using deuterium-proton contrast methods one can then obtain pseudo-high-resolution proton spectra of peptides or proteins embedded in deuterated membranes and determine their atomic 3D structure using quasi-conventional liquid-state NMR methods.
Sizun
Christina
C
Institut Européen de Chimie et Biologie, Ecole Polytechnique, 2 rue Robert Escarpit, 33607 Pessac, France.
Aussenac
Fabien
F
Grelard
Axelle
A
Dufourc
Erick J
EJ
D002722:Chlorobenzenes / Q000737:chemistry; D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry; D004745:Enkephalins / Q000737:chemistry; D006634:Histamine H1 Antagonists / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008823:Micelles; D008958:Models, Molecular; D015513:Oncogene Proteins / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D020794:Receptor Protein-Tyrosine Kinases
D002722:Chlorobenzenes; D004745:Enkephalins; D006634:Histamine H1 Antagonists; D008823:Micelles; D015513:Oncogene Proteins; D010455:Peptides; D020794:Receptor Protein-Tyrosine Kinases; C004944:chlorfenethol; D004134:Dimyristoylphosphatidylcholine