## Abstract In an attempt to account for the preferential binding to nonactin of K^+^ relative to Na^+^, theoretical computations are performed using the intermolecular interaction energies of the ionophore with the two cations. Both K^+^ and Na^+^ liganding conformations are considered, and an eva
β¦ LIBER β¦
The K+-ionophores nonactin and valinomycin interact differently with the protein of reconstituted cytochromecoxidase
β Scribed by Dietmar Steverding; Bernhard Kadenbach
- Publisher
- Springer US
- Year
- 1990
- Tongue
- English
- Weight
- 375 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0145-479X
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Theoretical study of the interaction of
β
Nohad Gresh; Alberte Pullman
π
Article
π
1982
π
John Wiley and Sons
π
English
β 437 KB
Studies on the interaction of protein wi
β
Wei Sun; Junying Han; Kui Jiao; Lude Lu
π
Article
π
2006
π
Elsevier Science
π
English
β 265 KB
Interaction of polypeptides with the gas
β
John Cuppoletti; Danuta H. Malinowska
π
Article
π
1992
π
Springer
π
English
β 525 KB
The 26 amino acid bee venom toxin, melittin, is an amphipathic helical polypeptide which inhibits the gastric (H+ + K+)ATPase. The site of interaction with the (H+ + K+)ATPase was shown to be the alpha subunit of the (H+ + K+)ATPase in studies using [125I]azidosalicylyl melittin, a radioactive photo
Classical genetics and site directed mut
β
P Cossart; M-C Serre; B Gicquel-Sanzey; R Ebright; J Beckwith
π
Article
π
1986
π
Elsevier Science
π
English
β 135 KB
The effects of some protein-modifying re
β
Doz. Dr. J. Ε marda; L. MacholΓ‘n
π
Article
π
1988
π
John Wiley and Sons
π
English
β 586 KB
The effects of some protein-modifying reagents on the interaction of colicins A, E2, E3 and K with their respective Escherichia coli cell receptors') J. SMARDA and L
Interaction of Mg(II), Ca(II) and Mn(II)
β
A. Ahmed; H.A. Tajmir-Riahi
π
Article
π
1994
π
Elsevier Science
π
English
β 632 KB