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Publikováno v:
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
The outer membrane protein F (OmpF) is known to play an important role in the uptake of fluoroquinolone antibiotics by bacteria. In this study, the degree of binding of the fluoroquinolone antibiotic ciprofloxacin to OmpF in a lipid membrane environm
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. (9):1976-1986
The membrane location of two fragments in two different K(+)-channels, the KvAP (from Aeropyrum pernix) and the HsapBK (human) corresponding to the putative "paddle" domains, has been investigated by CD, fluorescence and NMR spectroscopy. Both domain
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. (12):3069-3077
We examined the volumetric behavior of the dipalmitoylphosphatidylcholine (DPPC)/cholesterol binary bilayer system with high accuracy and more cholesterol concentrations to reveal the detailed molecular states in the liquid-disordered (Ld) phase, the
Autor:
Yasushi Ishihama, Hirofumi Shimizu, Shigetoshi Oiki, Hiroyuki Nakao, Masayuki Iwamoto, Minoru Nakano, Keisuke Ikeda
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. (1):145-150
KcsA is a pH-dependent potassium channel that is activated at acidic pH. The channel undergoes global conformational changes upon activation. We hypothesized that the open–close conformational changes of the transmembrane region could promote the f