Balázs Majer - Academia.edu (original) (raw)

Papers by Balázs Majer

Research paper thumbnail of Analysis of clones of Pinots grown in Hungary by SSR markers

Scientia Horticulturae, 2011

Based on our former experiences 7 Pinot gris, 4 Pinot noir clones and Pinot blanc were analysed i... more Based on our former experiences 7 Pinot gris, 4 Pinot noir clones and Pinot blanc were analysed in 16 (VVS2, VMC5E9, VMC3D12, VVIM10, VMC5G8, VMCNG1E1, VMC1F10, VMC2H4, VMC8A7, VMC7G3, VVMD28, VrZag21, VrZag79, VMC1C10, VrZag25, Scu06vv) microsatellite loci. A dendogramm was constructed using the shared allele method for the estimates of genetic similarity between pairs, and the neighbour joining method for clustering. Based on our results, it can be established, that the Pinot clones all showed high similarity. The Pinot gris clones bred in Badacsony, Hungary (B. 10, B. 10/5, B. 10/10) formed a group and showed the highest similarity with Pinot gris 34 from Romania. The other Pinot gris clones formed another group with Pinot noir C-162. These clones all originated from Western Europe (Germany, France). These genetic differences could be traced back to the different geographical origin of the different clones.

Research paper thumbnail of Effect of d-amino acids at Asp 23 and Ser 26 residues on the conformational preference of Aβ 20–29 peptides

Biochemical and Biophysical Research Communications, 2005

The effects of D-amino acids at Asp 23 and Ser 26 residues on the conformational preference of b-... more The effects of D-amino acids at Asp 23 and Ser 26 residues on the conformational preference of b-amyloid (Ab) peptide fragment (Ab 20-29 ) have been studied using different spectroscopic techniques, namely vibrational circular dichroism (VCD), vibrational absorption, and electronic circular dichroism. To study the structure of the Ab 20-29 , [D-Asp 23 ]Ab 20-29 , and [D-Ser 26 ]Ab 20-29 peptides under different conditions, the spectra were measured in 10 mM acetate buffer (pH 3) and in 2,2,2-trifluoroethanol (TFE). The spectroscopic results indicated that at pH 3, Ab 20-29 peptide takes random coil with b-turn structure, while [D-Ser 26 ]Ab 20-29 peptide adopts significant amount of polyproline II (PPII) type structure along with b-turn contribution and D-Asp-substituted peptide ([D-Asp 23 ]Ab 20-29 ) adopts predominantly PPII type structure. The increased propensity for PPII conformation upon D-amino acid substitution, in acidic medium, has important biological implications. In TFE, Ab 20-29 , [D-Asp 23 ]Ab 20-29 , and [D-Ser 26 ]Ab 20-29 peptides adopt 3 10 -helix, a-helix, and random coil with some b-turn structures, respectively. The VCD data obtained for the Ab peptide films suggested that the secondary structures for the peptide films are not the same as those for corresponding solution and are also different among the Ab peptides studied here. This observation suggests that dehydration can have a significant influence on the structural preferences of these peptides.

Research paper thumbnail of Analysis of clones of Pinots grown in Hungary by SSR markers

Scientia Horticulturae, 2011

Based on our former experiences 7 Pinot gris, 4 Pinot noir clones and Pinot blanc were analysed i... more Based on our former experiences 7 Pinot gris, 4 Pinot noir clones and Pinot blanc were analysed in 16 (VVS2, VMC5E9, VMC3D12, VVIM10, VMC5G8, VMCNG1E1, VMC1F10, VMC2H4, VMC8A7, VMC7G3, VVMD28, VrZag21, VrZag79, VMC1C10, VrZag25, Scu06vv) microsatellite loci. A dendogramm was constructed using the shared allele method for the estimates of genetic similarity between pairs, and the neighbour joining method for clustering. Based on our results, it can be established, that the Pinot clones all showed high similarity. The Pinot gris clones bred in Badacsony, Hungary (B. 10, B. 10/5, B. 10/10) formed a group and showed the highest similarity with Pinot gris 34 from Romania. The other Pinot gris clones formed another group with Pinot noir C-162. These clones all originated from Western Europe (Germany, France). These genetic differences could be traced back to the different geographical origin of the different clones.

Research paper thumbnail of Effect of d-amino acids at Asp 23 and Ser 26 residues on the conformational preference of Aβ 20–29 peptides

Biochemical and Biophysical Research Communications, 2005

The effects of D-amino acids at Asp 23 and Ser 26 residues on the conformational preference of b-... more The effects of D-amino acids at Asp 23 and Ser 26 residues on the conformational preference of b-amyloid (Ab) peptide fragment (Ab 20-29 ) have been studied using different spectroscopic techniques, namely vibrational circular dichroism (VCD), vibrational absorption, and electronic circular dichroism. To study the structure of the Ab 20-29 , [D-Asp 23 ]Ab 20-29 , and [D-Ser 26 ]Ab 20-29 peptides under different conditions, the spectra were measured in 10 mM acetate buffer (pH 3) and in 2,2,2-trifluoroethanol (TFE). The spectroscopic results indicated that at pH 3, Ab 20-29 peptide takes random coil with b-turn structure, while [D-Ser 26 ]Ab 20-29 peptide adopts significant amount of polyproline II (PPII) type structure along with b-turn contribution and D-Asp-substituted peptide ([D-Asp 23 ]Ab 20-29 ) adopts predominantly PPII type structure. The increased propensity for PPII conformation upon D-amino acid substitution, in acidic medium, has important biological implications. In TFE, Ab 20-29 , [D-Asp 23 ]Ab 20-29 , and [D-Ser 26 ]Ab 20-29 peptides adopt 3 10 -helix, a-helix, and random coil with some b-turn structures, respectively. The VCD data obtained for the Ab peptide films suggested that the secondary structures for the peptide films are not the same as those for corresponding solution and are also different among the Ab peptides studied here. This observation suggests that dehydration can have a significant influence on the structural preferences of these peptides.