Zobrazeno 1 - 5
of 5
pro vyhledávání: '"N. B. Il'ina"'
Autor:
N. B. Il’ina, Vitaly A. Balobanov, Dmitry A. Dolgikh, V. E. Bychkova, I. A. Kashparov, N. S. Katina
Publikováno v:
Molecular Biology. 44:624-632
The interaction of apomyoglobin and its mutant forms with phospholipid membranes was studied using tryptophan fluorescence and circular dichroism in the far UV region. It is shown that a negatively charged phospholipid membrane can have a dual effect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0b210fade9505c89a74dfac1741728c8
https://doi.org/10.1134/s0026893310040187
https://doi.org/10.1134/s0026893310040187
Publikováno v:
Molecular Biology. 36:718-725
Cytochrome b5 is a membrane protein that comprises two fragments: one is water-soluble and heme-containing, and the other is hydrophobic and membrane-embedded. The function of electron transfer is performed by the former whose crystal structure is kn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1892d0f09727dd170ba19147b3511786
https://doi.org/10.1023/a:1020687800727
https://doi.org/10.1023/a:1020687800727
Publikováno v:
Molekuliarnaia biologiia. 44(4)
The interaction of apomyoglobin and its mutant forms with phospholipid membranes was studied using tryptophan fluorescence and CD in the far UV-region. It is shown that a negatively charged phospholipid membrane can have a double effect on the struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a7e4ad60fc2e61cad45e3737bbe842c4
https://pubmed.ncbi.nlm.nih.gov/20873231
https://pubmed.ncbi.nlm.nih.gov/20873231
Publikováno v:
Molekuliarnaia biologiia. 39(2)
Equilibrium unfolding of apomyoglobin by urea was investigated in the temperature range from 5 to 25 degrees C at two pH values. The thermodynamic parameters of the apomyoglobin native-unfolded state transition were determined. Conformational changes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4a3744bfb5554e054d8e5e297a37a45e
https://pubmed.ncbi.nlm.nih.gov/15856957
https://pubmed.ncbi.nlm.nih.gov/15856957
Publikováno v:
Molekuliarnaia biologiia. 36(5)
Cytochrome b5 is a membrane protein that comprises two fragments: one is water-soluble and heme-containing, and the other is hydrophobic and membrane-embedded. The function of electron transfer is performed by the former whose crystal structure is kn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c47021f6310513f3026d60e0595892d6
https://pubmed.ncbi.nlm.nih.gov/12391854
https://pubmed.ncbi.nlm.nih.gov/12391854