F
Friedrich Lottspeich
Researcher at Max Planck Society
Publications - 449
Citations - 31053
Friedrich Lottspeich is an academic researcher from Max Planck Society. The author has contributed to research in topics: Peptide sequence & Amino acid. The author has an hindex of 94, co-authored 449 publications receiving 30250 citations. Previous affiliations of Friedrich Lottspeich include Technische Universität Darmstadt & University of Marburg.
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The further construction of the two-dimensional database of common human proteins.
TL;DR: The master two‐dimensional gel database of common human proteins has been expanded to include detailed protein characteristics and specific information regarding glycosylation and quantitation of expression levels after chemical, biological and mechanical stimulation is included in the database.
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Litomosoides carinii microfilarial sheaths: Partial amino-acid sequences of several major polypeptide constituents
Martin Hintz,Jörg Hirzmann,Gerd Hobom,Dietmar Linder,Friedrich Lottspeich,Hans-Henning Schott,Franz Josef Conraths,Horst Zahner,Stephan Stirm +8 more
TL;DR: A library of 27 partial sheath polypeptide sequences was established, 21 of which could be assigned to three L. carinii sheath structural genes isolated on the basis of this and of previous amino acid sequence information.
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Deletion of a B800-850 light-harvesting complex in Rhodospirillum molischianum DSM119 leads to "revertants" expressing a B800-820 complex: insights into pigment binding
TL;DR: A B800-850 light-harvesting complex of Rhodospirillum molischianum and Rhodopseudomonas acidophila reveals a conserved motif comprised of three amino acid residues which might be important for the precise structural arrangement of the native complex and fine tuning of its spectroscopic properties.
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Structural aspects on the glycosylation sites in human fibrinogen.
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The DNA polymerase-encoding gene from a thermoacidophilic archaeon Sulfolobus acidocaldarius.
Nelly Datukishvili,D K Pokholok,Friedrich Lottspeich,David Prangishvili,Vladimir O. Rechinsky +4 more
TL;DR: All conserved motifs characteristic of family B of DNA polymerases have been found in the deduced primary structure of this enzyme.