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NMR processing:
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Ab initio:
GeNMR
Cyana
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Fragment-based:
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Refinement:
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Torsion angles from chemical shifts:
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From structure:
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From sequence:
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Default Asp85 is the only internal aspartic acid that gets protonated in the M intermediate a

Asp85 is the only internal aspartic acid that gets protonated in the M intermediate and the purple-to-blue transition of bacteriorhodopsin. A solid-state 13C CP-MAS NMR investigation.

Related Articles Asp85 is the only internal aspartic acid that gets protonated in the M intermediate and the purple-to-blue transition of bacteriorhodopsin. A solid-state 13C CP-MAS NMR investigation.

FEBS Lett. 1992 Jun 1;303(2-3):237-41

Authors: Metz G, Siebert F, Engelhard M

High-resolution solid-state 13C NMR spectra of the ground state and M intermediate of the bacteriorhodopsin mutant D96N with the isotope label at [4-13C]Asp and [11-13C]Trp were recorded. The NMR spectra show that Asp85 is protonated in the M intermediate. The environment of Asp85 is quite hydrophobic. On the other hand, Asp212 remains deprotonated and a slight shift to lower field indicates a more hydrophilic environment. Asp85 also protonates in the purple-to-blue transition of bacteriorhodopsin in the deionized membrane, where it experiences a similar environment to M. The shift of Trp resonances in M reflect a conformational change of the protein in forming the M intermediate.

PMID: 1318849 [PubMed - indexed for MEDLINE]



Source: PubMed
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