Abstract
Recently, there has been great interest in determining the three-dimensional structures of membrane proteins, particularly bacteriorhodopsin, for which a variety of possible folding arrangements have been suggested1-4. In this paper we present nuclear magnetic resonance (NMR) spectra5-8 of deuterated bacteriorhodopsin, and use the data to help interpret the various suggested bacteriorhodopsin folding patterns. The results strongly indicate that (1) a membrane surface (±1 residue) may be defined by NMR in bacteriorhodopsin; (2) all amino acids inside the surface are essentially crystalline; (3) all amino acids outside the surface (surface residues) in bacteriorhodopsin are highly mobile on the time scale of the 2H NMR experiments; (4) NMR data may be used to help evaluate the various structural models that have been proposed; (5) aggregation of purple membrane sheets may lead to an immobilization of the surface residues.
Original language | English (US) |
---|---|
Pages (from-to) | 383-386 |
Number of pages | 4 |
Journal | Nature |
Volume | 307 |
Issue number | 5949 |
DOIs | |
State | Published - 1984 |
ASJC Scopus subject areas
- General