ISSN:
1573-5001
Schlagwort(e):
Bacteriorhodopsin
;
Structure
;
Membrane proteins
;
Isotope labelling
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
,
Chemie und Pharmazie
Notizen:
Abstract 1H NMR signals of the retinal moiety in detergent-solubilizedbacteriorhodopsin are assigned, enabling the interpretation of NOEs within thechromophore. To achieve this, a number of differently labelled samples wereprepared to test the applicability of the various assignment and distancemeasurement strategies. In measurements with and without light,1H and 13C chemical shifts of the retinal in thenative protein were partially assigned for both the dark- and thelight-adapted states. Additionally, samples with residue-specific1H amino acids and/or retinal in an otherwise deuterated proteinwere prepared to measure the distances between either two kinds of amino acidsor between individual amino acids and the retinal moiety. With the observationof NOE within the bound retinal and between retinal and its neighbouring aminoacids, an important step towards the elucidation of distance constraints inthe binding pocket of the proton pump is made.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1023/A:1018300215322
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