�ber das ?Chorionepithelioma malignum?

Huber, Herbert; Hörmann, Georg

doi:10.1007/bf00524615

Cited by 15 publications

(2 citation statements)

References 25 publications

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“…A self‐rotation search was performed using the Crystallography & NMR System (CNS) software package (Brünger et al ., 1998) to locate a possible non‐crystallographic dyad axis relating the molecules in the asymmetric unit. A real‐space Patterson‐search method (Huber, 1995) was employed using data in the resolution range 15.0–4.0 Å and the unique axis along b . The self‐rotation function was carried out by varying ψ and φ spherical polar angles in steps of 2° in the range ψ = 0–180°, φ = 0–180° while restricting κ, the rotation angle around the putative non‐crystallographic rotation axis, to 160°–180°.…”

Section: Methodsmentioning

confidence: 99%

Structure-specific tRNA-binding protein from the extreme thermophile Aquifex aeolicus

Morales

1999

The EMBO Journal

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The genome of the bacterium Aquifex aeolicus encodes a polypeptide which is related to a small portion of a sequence found in one prokaryotic and two eukaryotic tRNA synthetases. It also is related to a portion of Arc1p, a tRNA-binding protein believed to be important for nuclear trafficking of tRNAs. Here we cloned, expressed and purified the 111 amino acid polypeptide (designated Trbp111) and showed by ultracentrifugation analysis that it is a stable dimer in solution. The protein was also crystallized in a monoclinic lattice. X-ray diffraction analysis at 2.8 Å resolution revealed a prominent non-crystallographic 2-fold axis, consistent with the presence of a symmetric homodimeric structure. Band-shift analysis with polyacrylamide gels showed that the dimer binds tRNAs, but not RNA duplexes, RNA hairpins, single-stranded RNA nor 5S rRNA. Complex formation with respect to tRNA is non-specific, with a single tRNA bound per dimer. Thus, Trbp111 is a structure-specific tRNA-binding protein. These results and other considerations raise the possibility that Trbp111 is a tRNA-specific chaperone which stabilizes the native L-shaped fold in the extreme thermophile and which has been incorporated into much larger tRNA-binding proteins of higher organisms.

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Section: Methodsmentioning

confidence: 99%

Structure-specific tRNA-binding protein from the extreme thermophile Aquifex aeolicus

Morales

1999

The EMBO Journal

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“…Als erste, unseres Wissens einzige Verbindung wurde Ph3PbSCH2CH2OH (4) durch Umsetzung von PhaPbCl mit HSCH2CH2OH (1) in Gegenwart von Base dargestellt [1]; Ph2Pb(SCH2CH2)2 konnte auf diesem Wege nicht gewonnen werden [1]. Wir beobachteten, daß Bleitetraethyl und 1 in Abwesenheit eines Lösungsmittels bei 50 °C nicht reagierten, daß jedoch aus benzolischer Lösung schon bei Raumtemperatur als Zersetzungsprodukt Pb(SCH2CH2OH)2 ausfiel [2].…”

unclassified

(Hydroxyalkyl)- und (4-Hydroxyphenyl)- organoplumbylsulfide / (Hydroxyalkyl)- and (4-Hydroxyphenyl)-organoplumbyl Sulfides

Hager

Huber

1980

Zeitschrift Für Naturforschung B

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Ph3PbOH (Ph = C6H5), (Ph2Pb)2O or Me2Pb(OH)2 (Me = CH3) and 2-mercaptoethanol (1), 3-mercaptopropandiol-1,2 (2) or 4-mercaptophenol (3) react in CHCl3 or ether to give Ph3PbSR′OH [R′ = CH2CH2 (4), CH2CHOHCH2 (5), C6H4], Ph2Pb(SR′OH)2 [R′ = CH2CH2 (7), CH2CHOHCH2(8),C6H4]and Me2Pb(SC6H4OH)2. According to spectroscopic data the ligands are bonded to tetracoordinated Pb through S, the molecules being H-bonded in the solid state. 7 redistributes above - 20 °C to give 4, (SR′OH)2 and Pb(SCH2CH2OH)2, 8 redistributes to give 5, 2, (SR′OH)2, and Pb(SCH2CHOHCH2O)

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Trophoblasttumoren

Leppien¹,

Rabe²

1987

Gynäkologische Endokrinologie

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�ber das ?Chorionepithelioma malignum?

Cited by 15 publications

References 25 publications

Structure-specific tRNA-binding protein from the extreme thermophile Aquifex aeolicus

Structure-specific tRNA-binding protein from the extreme thermophile Aquifex aeolicus

(Hydroxyalkyl)- und (4-Hydroxyphenyl)- organoplumbylsulfide / (Hydroxyalkyl)- and (4-Hydroxyphenyl)-organoplumbyl Sulfides

Trophoblasttumoren

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