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EnglishResonance Raman spectra of the native Lhcb4 antenna protein are compared with those of a recombinant protein prepared by in vitro refolding of its polypeptide, over-expressed in Escherichia coli, with added pigments [Giuffra et al. (1996) Eur. J. Biochem. 238, 112-120]. The results indicate that the native pigment conformation is reproduced almost perfectly in the reconstituted protein, with only small differences which are attributed to a slight shift in the Soret absorption peak of two or more chlorophylls. This procedure therefore represents a model system for the investigation of site-directed mutant LHC proteins, which are otherwise very difficult to obtain.
| Titolo: | Pigment conformation and pigment-protein interactions in the reconstituted Lhcb4 antenna protein | |
| Autori: | ||
| Data di pubblicazione: | 2000 | |
| Rivista: | ||
| Abstract: | Resonance Raman spectra of the native Lhcb4 antenna protein are compared with those of a recombinant protein prepared by in vitro refolding of its polypeptide, over-expressed in Escherichia coli, with added pigments [Giuffra et al. (1996) Eur. J. Biochem. 238, 112-120]. The results indicate that the native pigment conformation is reproduced almost perfectly in the reconstituted protein, with only small differences which are attributed to a slight shift in the Soret absorption peak of two or more chlorophylls. This procedure therefore represents a model system for the investigation of site-directed mutant LHC proteins, which are otherwise very difficult to obtain. | |
| Handle: | http://hdl.handle.net/11562/14941 | |
| Appare nelle tipologie: | 01.01 Articolo in Rivista |
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