Abstract
Proton-NMR studies of native bacteriorhodopsin revealed the existence of about nine relatively mobile aromatic residues out of the 32 totally present in the protein. These nine comprise approximately three tyrosines, two tryptophans and four phenylalanines. Photo-CIDNP data strongly suggest that, aside from phenylalanines, only one tyrosine and one tryptophan residue are exposed to the solvent. These data are discussed in terms of the current structural model for bacteriorhodopsin.
Original language | English |
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Pages (from-to) | 163-168 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 235 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 1 Aug 1988 |
Keywords
- Bacteriorhodopsin
- Membrane protein
- NMR
- Photo-CIDNP
- Proton nuclear resonance
- Side-chain mobility
- exposure
- model
- nuclear magnetic resonance spectroscopy
- proton nuclear magnetic resonance
- bacteriorhodopsin
- solvent