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Wyświetlanie 1-3 z 3
Tytuł:
Attaching a spin to a protein - site-directed spin labeling in structural biology
Autorzy:
Czogalla, Aleksander
Pieciul, Aldona
Jezierski, Adam
Sikorski, Aleksander
Powiązania:
https://bibliotekanauki.pl/articles/1041067.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protein structure
site-directed spin labeling
electron paramagnetic resonance (EPR) spectroscopy
Opis:
Site-directed spin labeling and electron paramagnetic resonance spectroscopy have recently experienced an outburst of multiple applications in protein science. Numerous interesting strategies have been introduced for determining the structure of proteins and its conformational changes at the level of the backbone fold. Moreover, considerable technical development in the field makes the technique an attractive approach for the study of structure and dynamics of membrane proteins and large biological complexes at physiological conditions. This review focuses on a brief description of site-directed spin labeling-derived techniques in the context of their recent applications.
Źródło:
Acta Biochimica Polonica; 2007, 54, 2; 235-244
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Interaction of membrane skeletal proteins with membrane lipid domain.
Autorzy:
Sikorski, Aleksander
Hanus-Lorenz, Beata
Jezierski, Adam
Dluzewski, Anton
Powiązania:
https://bibliotekanauki.pl/articles/1044290.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
non-erythroid cells
membrane skeleton
membrane lipid domains
cytoskeleton
red blood cells
Opis:
The object of this paper is to review briefly the studies on the interaction of red blood cell membrane skeletal proteins and their non-erythroid analogues with lipids in model systems as well as in natural membranes. An important question to be addressed is the physiological significance and possible regulatory molecular mechanisms in which these interactions are engaged.
Źródło:
Acta Biochimica Polonica; 2000, 47, 3; 565-578
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Expression, purification and functional characterization of recombinant human acyl-CoA-binding protein (ACBP) from erythroid cells
Autorzy:
Augoff, Katarzyna
Kolondra, Adam
Chorzalska, Anna
Lach, Agnieszka
Grabowski, Krzysztof
Sikorski, Aleksander
Powiązania:
https://bibliotekanauki.pl/articles/1040319.pdf
Data publikacji:
2010
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
acyl-CoA-binding protein
PC
DBI
ACBP
phosphatidylcholine
Opis:
Fatty acyl-CoA esters are extremely important in cellular homeostasis. They are intermediates in both lipid metabolism and post-translational protein modifications. Among these modification events, protein palmitoylation seems to be unique by its reversibility which allows dynamic regulation of the protein hydrophobicity. The recent discovery of an enzyme family that catalyze protein palmitoylation has increased the understanding of the enzymology of the covalent attachment of fatty acids to proteins. Despite that, the molecular mechanism of supplying acyl-CoA esters to this reaction is yet to be established. Acyl-coenzyme A-binding proteins are known to bind long-chain acyl-CoA esters with very high affinity. Therefore, they play a significant role in intracellular acyl-CoA transport and pool formation. The purpose of this work is to explore the potential of one of the acyl-CoA-binding proteins to participate in the protein palmitoylation. In this study, a recombinant form of ACBP derived from human erythroid cells was expressed in E. coli, purified, and functionally characterized. We demonstrate that recombinant hACBP effectively binds palmitoyl-CoA in vitro, undergoing a shift from a monomeric to a dimeric state, and that this ligand-binding ability is involved in erythrocytic membrane phosphatidylcholine (PC) remodeling but not in protein acylation.
Źródło:
Acta Biochimica Polonica; 2010, 57, 4; 533-540
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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