In the wild-type chlorosomes, the BChl stacks are oriented in the direction of the long axis. Again a helical O–H···O=C exciton delocalization pathway is present, with opposite handedness as compared to the bchQRU mutant. The observed spacing of 1.25 nm (Fig. 4a, b) in this configuration is directly related to the size of a syn-anti heterodimer, the basic
repeating unit, in the direction of the stack. Simulated projection images from these nanotube models and Fourier analysis confirmed that the supramolecular models were consistent with the experimental data (Fig. 7). Fig. 6 Molecular models of BChl syn-anti monomer stacks in tubular models of a a single stack showing the farnesyl tails alternately extending on both sides. Radius of Selleckchem GSK1210151A {Selleck Anti-diabetic Compound Library|Selleck Antidiabetic Compound Library|Selleck Anti-diabetic Compound Library|Selleck Antidiabetic Compound Library|Selleckchem Anti-diabetic Compound Library|Selleckchem Antidiabetic Compound Library|Selleckchem Anti-diabetic Compound Library|Selleckchem Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|buy Anti-diabetic Compound Library|Anti-diabetic Compound Library ic50|Anti-diabetic Compound Library price|Anti-diabetic Compound Library cost|Anti-diabetic Compound Library solubility dmso|Anti-diabetic Compound Library purchase|Anti-diabetic Compound Library manufacturer|Anti-diabetic Compound Library research buy|Anti-diabetic Compound Library order|Anti-diabetic Compound Library mouse|Anti-diabetic Compound Library chemical structure|Anti-diabetic Compound Library mw|Anti-diabetic Compound Library molecular weight|Anti-diabetic Compound Library datasheet|Anti-diabetic Compound Library supplier|Anti-diabetic Compound Library in vitro|Anti-diabetic Compound Library cell line|Anti-diabetic Compound Library concentration|Anti-diabetic Compound Library nmr|Anti-diabetic Compound Library in vivo|Anti-diabetic Compound Library clinical trial|Anti-diabetic Compound Library cell assay|Anti-diabetic Compound Library screening|Anti-diabetic Compound Library high throughput|buy Antidiabetic Compound Library|Antidiabetic Compound Library ic50|Antidiabetic Compound Library price|Antidiabetic Compound Library cost|Antidiabetic Compound Library solubility dmso|Antidiabetic Compound Library purchase|Antidiabetic Compound Library manufacturer|Antidiabetic Compound Library research buy|Antidiabetic Compound Library order|Antidiabetic Compound Library chemical structure|Antidiabetic Compound Library datasheet|Antidiabetic Compound Library supplier|Antidiabetic Compound Library in vitro|Antidiabetic Compound Library cell line|Antidiabetic Compound Library concentration|Antidiabetic Compound Library clinical trial|Antidiabetic Compound Library cell assay|Antidiabetic Compound Library screening|Antidiabetic Compound Library high throughput|Anti-diabetic Compound high throughput screening| curvature 10.2 nm. b Two syn-anti stacks interconnected by hydrogen bonds (black dotted line in the centre). The orange arrow indicates the direction of the exciton delocalization pathway over neighbouring stacks along the connecting hydrogen bonds. The models were made in Swiss-PDB Viewer and visualized using Pymol Fig. 7 Cylindrical model of the packing of concentric lamellae in the Chlorobaculum tepidum bchQRU mutant, based on distances
as observed by electron microscopy and solid-state NMR spectroscopy (Ganapathy et al. 2009). The spacing between layers is 2.1 nm. The green band indicates the position of individual Bchl molecules in four stacks of syn-anti dimers. In the wild-type chlorosomes, the stacks run in the direction of the cylinder axis Organization of the baseplate The chlorosome baseplate was first described as a 2D para-crystalline structure by freeze-fracture electron microscopy (Staehelin et al. 1980). It may be a monolayer of polar lipids, like the chlorosome envelope. Besides polar lipids, BIX 1294 chemical structure chlorosomes also contain non-polar lipids
(waxes) (Sørensen et al. 2008), but their location is completely unknown. About 10 different proteins are embedded in the base plate. Among these, the most abundant is the 59-residue chlorosome protein A (CsmA). The structure of apo-CsmA from C. tepidum was determined using NMR spectroscopy (Østergaard Pedersen et al. 2008). Overall, the 59-residue CsmA is predominantly α-helical in nature with a long helical domain extending from residue 6–36, containing a putative BChl a binding domain, and a short helix in the C-terminal part many extending from residue 41–49. The long N-terminal α-helical stretch is considered to be immersed into the lipid monolayer confining the chlorosome, whereas the short C-terminal helix is protruding outwards, thus supposedly being available for interaction with the FMO antenna protein. CsmA is known to form stable oligomers in the chlorosome baseplate (Li et al. 2006). In order to assemble two BChl a molecules in close connection, it was proposed that in the intact baseplate of the C. tepidum chlorosomes, CsmA exists as dimers (Østergaard Pedersen et al.