V
Volker Kruft
Researcher at Applied Biosystems
Publications - 54
Citations - 3303
Volker Kruft is an academic researcher from Applied Biosystems. The author has contributed to research in topics: Peptide sequence & Ribosomal protein. The author has an hindex of 29, co-authored 54 publications receiving 3212 citations. Previous affiliations of Volker Kruft include Max Delbrück Center for Molecular Medicine & Max Planck Society.
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Proteomic Approach to Identify Novel Mitochondrial Proteins in Arabidopsis
TL;DR: The map of the Arabidopsis mitochondrial proteome should be useful for the analysis of knockout mutants concerning nuclear-encoded mitochondrial genes, indicating novel mitochondrial functions in plants.
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The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain.
TL;DR: The major mitochondrial processing activity removing presequences from nuclear encoded precursor proteins is present in the soluble fraction of fungal and mammalian mitochondria and it is found that in potato, this activity resides in the inner mitochondrial membrane.
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New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria
TL;DR: BN-PAGE allows the preparation of mitochondrial protein complexes from gram amounts of plant tissue, as the procedure only requires milligram amounts of organelles and reveals novel results for their composition, molecular mass and stoichiometry.
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The Multiple Carrier Model of Nonribosomal Peptide Biosynthesis at Modular Multienzymatic Templates
Torsten Stein,Joachim Vater,Volker Kruft,Albrecht Otto,Brigitte Wittmann-Liebold,Peter Franke,Maria Panico,Roy A. McDowell,Howard R. Morris +8 more
TL;DR: It was demonstrated that a 4′-phosphopantetheine cofactor is attached to the central serine of the thiolation motif in each amino acid-activating module of the gramicidin S synthetase multienzyme system forming the thioester binding sites for the amino acid substrates and catalyzing the elongation process.
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Purification and Characterization of the Preprotein Translocase of the Outer Mitochondrial Membrane from Arabidopsis. Identification of Multiple Forms of TOM20
TL;DR: The purification of this protein complex from Arabidopsis showed the presence of further forms of TOM20, which comprises a large cytoplasmically exposed hydrophilic domain, which is degraded upon trypsination of intact mitochondria.