Temat: circular dichroism spectroscopy - Katalog OPAC zbiorów

Skocz do pozycji: 1.

Tytuł:: How to study G-quadruplex structures
Autorzy:: Malgowska, M.
Gudanis, D.
Teubert, A.
Dominiak, G.
Gdaniec, Z.
Powiązania:: https://bibliotekanauki.pl/articles/80131.pdf
Data publikacji:: 2012
Wydawca:: Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:: guanine
DNA molecule
RNA molecule
molecular structure
intramolecular structure
intermolecular structure
G-quadruplex structure
circular dichroism spectroscopy
ultraviolet spectroscopy
electrospray ionization mass spectrometry
nuclear magnetic resonance
Źródło:: BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2012, 93, 4
0860-7796
Pojawia się w:: BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:: Biblioteka Nauki

Artykuł

Skocz do pozycji: 2.

Tytuł:: Protein thermal stabilization in aqueous solutions of osmolytes
Autorzy:: Bruździak, Piotr
Panuszko, Aneta
Jourdan, Muriel
Stangret, Janusz
Powiązania:: https://bibliotekanauki.pl/articles/1038842.pdf
Data publikacji:: 2016
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: water structure
protein stability
circular dichroism
FT-IR spectroscopy
DFT calculations
Opis:: Proteins' thermal stabilization is a significant problem in various biomedical, biotechnological, and technological applications. We investigated thermal stability of hen egg white lysozyme in aqueous solutions of the following stabilizing osmolytes: Glycine (GLY), N-methylglycine (NMG), N,N-dimethylglycine (DMG), N,N,N-trimethylglycine (TMG), and trimethyl-N-oxide (TMAO). Results of CD-UV spectroscopic investigation were compared with FTIR hydration studies' results. Selected osmolytes increased lysozyme's thermal stability in the following order: Gly>NMG>TMAO≈DMG>TMG. Theoretical calculations (DFT) showed clearly that osmolytes' amino group protons and water molecules interacting with them played a distinctive role in protein thermal stabilization. The results brought us a step closer to the exact mechanism of protein stabilization by osmolytes.
Źródło:: Acta Biochimica Polonica; 2016, 63, 1; 65-70
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

Artykuł

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