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Arthrospira maxima

The crystal structure of the OCP from Arthrospira maxima has been solved to 2.1 A resolution (Kerfeld et al. 2003). It is composed of two domains and the carotenoid, 3 -hydroxyechinenone, spans both. The carotenoid is almost completely buried within the protein only 3.4% of the pigment surface is accessible to solvent (see Figure 1.3a). The OCP is a dimer in solution the intermolecular interactions are largely mediated by hydrogen bonding among the N-terminal 30 amino acids, as shown in Figure 1.3b... [Pg.7]

Knutson, R. (1998). The red carotenoid protein from Arthrospira maxima. MS thesis, Purdue University, West Lafayette, IN. [Pg.16]

Polfvka, T., C. A. Kerfeld, T. Pascher, and V. Sundstrom (2005). Spectroscopic properties of the carotenoid 3 -hydroxyechinenone in the orange carotenoid protein from the cyanobacterium Arthrospira maxima. Biochemistry 44(10) 3994—4003. [Pg.17]

Sawaya MR, Krogmann DW, Serag A et al. Structures of cytochrome c-549 and cytochrome c6 from the cyanobacterium Arthrospira maxima. Biochemistry 2001 40 9215-9225. [Pg.31]


See other pages where Arthrospira maxima is mentioned: [Pg.35]    [Pg.820]    [Pg.822]    [Pg.824]    [Pg.825]    [Pg.826]    [Pg.828]    [Pg.829]    [Pg.831]    [Pg.833]    [Pg.834]    [Pg.835]    [Pg.837]    [Pg.840]    [Pg.841]    [Pg.844]    [Pg.248]   
See also in sourсe #XX -- [ Pg.67 ]




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Arthrospira

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