Wyniki wyszukiwania

1

The nucleotide sequence of ribosomal 5S RNA from Rhizobium meliloti: comparison with 5S rRNA of Agrobacterium

100%

Nalaskowska M., Barciszewska M., Barciszewski J.

Acta Biochimica Polonica

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1989

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tom 36

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nr 3-4

2

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Conformational changes in wheat gluten after using Ag-nanoparticles

100%

Nawrocka A.

International Agrophysics

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2014

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tom 28

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nr 3

3

The calculation of plant 5S rRNAs secondary structure

100%

Joachimiak A., Nalaskowska M., Barciszewska M. Z., Mashkova T. D., Barciszewski J.

Acta Biochimica Polonica

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1989

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tom 36

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nr 3-4

4

Circular dichroism and aggregation studies of amyloid beta [11-28] fragment and its variants

100%

Juszczyk P., Kolodziejczyk A. S., Grzonka Z.

Acta Biochimica Polonica

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2005

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tom 52

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nr 2

Aggregation of Aβ peptides is a seminal event in Alzheimer’s disease. Detailed understanding of Aβ assembly would facilitate the targeting and design of fibrillogenesis inhibitors. Here comparative conformational and aggregation studies using CD spectroscopy and thioflavine T fluorescence assay are presented. As a model peptide, the 11–28 fragment of Aβ was used. This model peptide is known to contain the core region responsible for Aβ aggregation. The structural and aggregational behaviour of the peptide was compared with the properties of its variants corresponding to natural, clinically relevant mutants at positions 21-23 (A21G, E22K, E22G, E22Q and D23N). In HFIP (hexafluoro-2-propanol), a strong α-helix inducer, the CD spectra revealed an unexpectedly high amount of β-sheet conformation. The aggregation process of Aβ(11–28) variants provoked by water addition to HFIP was found to be consistent with a model of an α-helix-containing intermediate. The aggregation propensity of all Aβ(11–28) variants was also compared and discussed.

5

Structural predication and antigenic analysis of Toxoplasma gondii ROP20

84%

Zhou J., Wang W., Song P., Wang L., Han Y., Guo J., Hao Z., Zhu X., Zhou Q., Du X., Lu G., He S., Luo Y.

Acta Parasitologica

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2018

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tom 63

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nr 2

6

Effect of tartaric acid on conformation and stability of human prostatic phosphatase: An infrared spectroscopic and calorimetric study

67%

Bem S., Ostrowski W. S.

Acta Biochimica Polonica

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2001

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tom 48

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nr 3

The solution structure and thermal stability of human prostatic acid phosphatase (hPAP) in the absence and in the presence of tartaric acid were studied by Fourier transform infrared spectroscopy (FTIR) and differential scanning calorimetry (DSC). The temperature dependence of the infrared spectrum and DSC scans indicate that hPAP undergoes thermal unfolding at a temperature between 49.5 and 52.5°C. Binding of tartaric acid does not lead to major changes in the secondary structure of hPAP, however, hPAP with bound tartaric acid shows a significantly increased thermal stability. These results helped to better understand the mechanism of hPAP unfolding at the elevated temperature.

Ograniczanie wyników

The nucleotide sequence of ribosomal 5S RNA from Rhizobium meliloti: comparison with 5S rRNA of Agrobacterium

Conformational changes in wheat gluten after using Ag-nanoparticles

The calculation of plant 5S rRNAs secondary structure

Circular dichroism and aggregation studies of amyloid beta [11-28] fragment and its variants

Structural predication and antigenic analysis of Toxoplasma gondii ROP20

Effect of tartaric acid on conformation and stability of human prostatic phosphatase: An infrared spectroscopic and calorimetric study