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- W2090439806 abstract "The structure of the chlorosome baseplate protein CsmA from Chlorobium tepidum in a 1:1 chloroform:methanol solution was determined using liquid‐state NMR spectroscopy. The data reveal that the 59‐residue protein is predominantly α‐helical with a long helical domain extending from residues V6 to L36, containing a putative bacteriochlorophyll a binding domain, and a short helix in the C‐terminal part extending from residues M41 to G49. These elements are compatible with a model of CsmA having the long N‐terminal α‐helical stretch immersed into the lipid monolayer confining the chlorosome and the short C‐terminal helix protruding outwards, thus available for interaction with the Fenna–Matthews–Olson antenna protein." @default.
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- W2090439806 date "2008-07-22" @default.
- W2090439806 modified "2023-10-15" @default.
- W2090439806 title "The three-dimensional structure of CsmA: A small antenna protein from the green sulfur bacterium<i>Chlorobium tepidum</i>" @default.
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- W2090439806 doi "https://doi.org/10.1016/j.febslet.2008.07.020" @default.
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