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Wyszukujesz frazę "Sulkowska, M." wg kryterium: Autor


Wyświetlanie 1-2 z 2
Tytuł:
Tests of the Structure-Based Models of Proteins
Autorzy:
Cieplak, M.
Sułkowska, J.
Powiązania:
https://bibliotekanauki.pl/articles/1808305.pdf
Data publikacji:
2009-02
Wydawca:
Polska Akademia Nauk. Instytut Fizyki PAN
Tematy:
87.80.Nj
87.15.ap
87.14.E-
Opis:
The structure-based models of proteins are defined through the condition that their ground state coincides with the native structure of the proteins. There are many variants of such models and they yield different properties. Optimal variants can be selected by making comparisons to experimental data on single-molecule stretching. Here, we discuss the 15 best performing variants and focus on fine tuning the selection process by adjusting the velocity of stretching to match the experimental conditions. The very best variant is found to correspond to the 10-12 potential in the native contacts with the energies modulated by the Miyazawa-Jernigan statistical potential and variable length parameters. The second best model incorporates the Lennard-Jones potential with uniform amplitudes. We then make a detailed comparison of the two models in which theoretical surveys of stretching properties of 7510 proteins were made previously.
Źródło:
Acta Physica Polonica A; 2009, 115, 2; 441-445
0587-4246
1898-794X
Pojawia się w:
Acta Physica Polonica A
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Comparative Analysis of KP-HSA Complex by Spectroscopic Methods
Autorzy:
Mąciażek-Jurczyk, M.
Równicka-Zubik, J.
Dyja, R.
Sułkowska, A.
Powiązania:
https://bibliotekanauki.pl/articles/1400125.pdf
Data publikacji:
2013-04
Wydawca:
Polska Akademia Nauk. Instytut Fizyki PAN
Tematy:
33.50.-j
33.50.Dq
82.56.-b
87.14.-g
87.14.E-
Opis:
The main objective of the presented study was to characterize the high (HAS) and low affinity (LAS) binding sites of ketoprofen (KP) in human serum albumin (HSA) structure with the use of spectrofluorescence and proton nuclear magnetic resonance spectroscopy. In vitro fluorescence analysis was used to estimate the effect of KP on the HSA fluorescence. The association constants $K_{a} [M^{-1}]$ of KP-HSA complex in the HAS were determined with the use of Scatchard, Klotz, and Hill analysis. The quenching $K_{Q} [M^{-1}]$ constants were determined on the basis of the Stern-Volmer equation. Binding of ketoprofen to plasma protein was also studied with the use of 8-anilinonapthalene-1-sulfonic acid (ANS) and 5-dimethylaminonaphthalene-1-sulfonic acid (DNSA) as the fluorescence probes in IIIA and IIA subdomains of HSA, respectively. To estimate the cooperativeness in proteins Hill's coefficient $n_{H}$ was used. The analysis of proton nuclear magnetic resonance spectra of KP in the presence of HSA allows us to observe the interactions between aromatic rings of the drug and the rings of amino acids located in the hydrophobic subdomains of the protein on the basis of the changes of chemical shifts Δ σ [ppm] of drug protons resonances. Moreover the $K_{a}$ constants $[M^{-1}]$ of KP-HSA complex in the LAS were determined.
Źródło:
Acta Physica Polonica A; 2013, 123, 4; 673-680
0587-4246
1898-794X
Pojawia się w:
Acta Physica Polonica A
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

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