The conformation of bacteriorhodopsin loops in purple membranes resolved by solid-state MAS NMR spectroscopy.
Κύριοι συγγραφείς: | Higman, V, Varga, K, Aslimovska, L, Judge, P, Sperling, L, Rienstra, C, Watts, A |
---|---|
Μορφή: | Journal article |
Γλώσσα: | English |
Έκδοση: |
2011
|
Παρόμοια τεκμήρια
Παρόμοια τεκμήρια
-
The conformation of bacteriorhodopsin loops in purple membranes resolved by solid-state MAS NMR spectroscopy
ανά: Higman, V, κ.ά.
Έκδοση: (2011) -
Advances towards resonance assignments for uniformly--13C, 15N enriched bacteriorhodopsin at 18.8 T in purple membranes.
ανά: Varga, K, κ.ά.
Έκδοση: (2008) -
Structural and orientational constraints of bacteriorhodopsin in purple membranes determined by oriented-sample solid-state NMR spectroscopy.
ανά: Kamihira, M, κ.ά.
Έκδοση: (2005) -
Deuterium-MAS NMR spectroscopy on oriented membrane proteins: Applications to photointermediates of bacteriorhodopsin
ανά: Glaubitz, C, κ.ά.
Έκδοση: (1999) -
Distorted structure of the retinal chromophore in bacteriorhodopsin resolved by 2H-NMR.
ανά: Ulrich, A, κ.ά.
Έκδοση: (1994)