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Use of fully deuterated micelles for conformational studies of membrane proteins by high resolution 1H nuclear magnetic resonance
Ist Teil von
Biochimica et biophysica acta. Biomembranes, 1979-10, Vol.557 (1), p.135-148
Ort / Verlag
Elsevier B.V
Erscheinungsjahr
1979
Link zum Volltext
Quelle
Elsevier Journal Backfiles on ScienceDirect (DFG Nationallizenzen)
Beschreibungen/Notizen
Micellar complexes of melittin with fully deuterated detergents have been studied by high resolution
1H nuclear magnetic resonance (NMR). The synthesis of deuterated micelles is described and it is shown that the
1H NMR spectrum of micelle-bound melittin is well resolved and suitable for detailed analysis by conventional high-resolution NMR methods. A preliminary characterization of micelle-bound melittin shows that interaction with the micelle results in different conformational and dynamic features for the hydrophobic and hydrophilic regions of the melittin amino acid sequence. The present experiments on melittin and preliminary results with other polypeptides and proteins demonstrate that in favourable cases high-resolution
1H NMR studies of the complexes formed between membrane proteins and deuterated micelles provides a viable method for conformational studies of membrane-bound proteins.