Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Dirk Meuser"'
Publikováno v:
FEBS Letters. 472:83-87
Designed mutations within the Streptomyces lividans kcsA gene resulted in a set of mutant proteins, which were characterized in respect to their assembly and channel activities. (i) The amino acid residue leucine 81 located at the external side of Kc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::746f319b24b755c54675a2dbda1ac739
https://doi.org/10.1016/s0014-5793(00)01429-0
https://doi.org/10.1016/s0014-5793(00)01429-0
Publikováno v:
FEBS Letters. 462:447-452
The tetrameric potassium channel from Streptomyces lividans (KcsA) embedded in planar bilayers exhibits the following electrophysiological characteristics: (i) K+ ions can cross the pore in a highly hydrated state (nH2Oor = 6), (ii) the selectivity f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d39f7bc5ea9b4639b2849ebbe260b08
https://doi.org/10.1016/s0014-5793(99)01579-3
https://doi.org/10.1016/s0014-5793(99)01579-3
Publikováno v:
European biophysics journal : EBJ. 30(5)
Four subunits of the bacterial Streptomyces lividans protein KcsA form a K+ channel which can be functionally reconstituted in vitro. Here we show that substitution of the tyrosine residue 82 by cysteine, valine or threonine, but not by glycine, led
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6afc258ac7db1dca689803eff5a79be
https://pubmed.ncbi.nlm.nih.gov/11592696
https://pubmed.ncbi.nlm.nih.gov/11592696