F
Franz Suter
Researcher at ETH Zurich
Publications - 58
Citations - 1951
Franz Suter is an academic researcher from ETH Zurich. The author has contributed to research in topics: Peptide sequence & Amino acid. The author has an hindex of 26, co-authored 58 publications receiving 1915 citations.
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Journal ArticleDOI
Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 Å resolution
Robert Huber,Monika Schneider,Irmgard Mayr,Rudi Müller,Rainer Deutzmann,Franz Suter,Herbert Zuber,Heinz Falk,Hartmut Kayser +8 more
TL;DR: The bilin binding protein from the insect Pieris brassicae has been analysed for amino acid sequence, spectral properties and three-dimensional structure and the fold of BBP is related to retinol binding protein (RBP), as had been recognized in the preliminary analysis.
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The complete amino acid sequence of the bacteriochlorophyll c binding polypeptide from chlorosomes of the green photosynthetic bacterium Chloroflexus aurantiacus
TL;DR: It appears that the BChl‐protein complex (chlorosome subunit, 5.2 × 6 nm) composed of 12 5.6 kDa polypeptides corresponds to the 'globular units' found by electron microscopy within the chlorosomes.
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The light-harvesting polypeptides of Rhodopseudomonas sphaeroides R-26.1. I. Isolation, purification and sequence analyses.
TL;DR: Four low-molecular-mass polypeptides were isolated and purified from chromatophore membranes of Rhodopseudomonas sphaeroides blue-green mutant R-26 by a combination of gel filtration and ion-exchange chromatography in organic solvents and revealed a tripartite structure.
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The light-harvesting polypeptides of Rhodospirillum rubrum. I. The amino-acid sequence of the second light-harvestng polypeptide B 880-beta (B 870-beta) of Rhodospirillum rubrum S 1 and the carotenoidless mutant G-9+. carotenoidless mutant G-9+.
TL;DR: The conserved histidine residue within the hydrophobic stretch raises more evidence for ligand complexation of bacteriochlorophyll to this specific histidine residues which therefore possibly plays the key role in pigment-protein interactions.
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The complete amino-acid sequence of both subunits of phycoerythrocyanin from the thermophilic cyanobacterium Mastigocladus laminosus.
TL;DR: The amino-acid sequences of both sub units of phycoerythrocyanin from the thermophilic cyanobacterium Mastigocladus laminosus have been determined and secondary structure predictions were calculated for all six subunits of the phycobiliproteins.