J
J. Steppuhn
Researcher at Ludwig Maximilian University of Munich
Publications - 17
Citations - 2192
J. Steppuhn is an academic researcher from Ludwig Maximilian University of Munich. The author has contributed to research in topics: Nucleic acid sequence & Peptide sequence. The author has an hindex of 15, co-authored 17 publications receiving 2170 citations.
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Journal ArticleDOI
Domain structure of mitochondrial and chloroplast targeting peptides.
TL;DR: Representative samples of mitochondrial and chloroplast targeting peptides have been analyzed in terms of amino acid composition, positional amino acid preferences and amphiphilic character and no highly conserved 'homology blocks' are found in either class of topogenic sequence.
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Nucleotide sequence of cDNA clones encoding the complete ‘23 kDa’ and ‘16 kDa’ precursor proteins associated with the photosynthetic oxygen-evolving complex from spinach
Thomas Jansen,C. Rother,J. Steppuhn,H. Reinke,K. Beyreuther,Christer Jansson,Bertil Andersson,Reinhold G. Herrmann +7 more
TL;DR: Primary structure predictions disclose epitopes that are potential candidates for two‐step processing of the precursors during import and intraorganelle routing as well as for calcium sequestering, chloride binding and subunit/subunit interaction.
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Nucleotide sequence of cDNA clones encoding the complete “33 kDa” precursor protein associated with the photosynthetic oxygen-evolving complex from spinach
TL;DR: The anatomy of the unusually long transit sequence is discussed with regard to current concepts of protein import into and protein routein within the organelle.
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Isolation of cDNA clones for fourteen nuclear-encoded thylakoid membrane proteins
Jochen Tittgen,Jürgen Hermans,J. Steppuhn,Thomas Jansen,Christer Jansson,Bertil Andersson,Rachel Nechushtai,Nathan Nelson,Reinhold G. Herrmann +8 more
TL;DR: Spinach cDNA libraries, made from polyadenylated seedling RNA, have been constructed in pBR322 and the expression vector λgt11 and contain components containing antigenic determinants against the lysine-rich 34 kd proteins.
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The ‘positive-inside rule’ applies to thylakoid membrane proteins
TL;DR: An analysis of proteins from the thylakoid membrane of chloroplasts is presented and it is shown that these proteins have the same charge asymmetry as has been reported for proteins from other membrane systems, with their more highly charged regions facing the stromal compartment.