Measurement of dipolar couplings in a uniformly (13)C,(15)N-labeled membrane protein: distances between the Schiff base and aspartic acids in the active site of bacteriorhodopsin.
Jaroniec
C P
CP
Department of Chemistry, Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Lansing
J C
JC
Tounge
B A
BA
Belenky
M
M
Herzfeld
J
J
Griffin
R G
RG
D001224:Aspartic Acid / Q000737:chemistry* / Q000378:metabolism; D001436:Bacteriorhodopsins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D002247:Carbon Isotopes; D004563:Electrochemistry; D019617:Halobacterium salinarum / Q000378:metabolism; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D018717:Purple Membrane / Q000737:chemistry / Q000378:metabolism
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D001224:Aspartic Acid; D001436:Bacteriorhodopsins