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Page 1
The lactose permease meets Frankenstein.
Kaback HR, Frillingos S, Jung H, Jung K, Privé GG, Ujwal ML, Weitzman C, Wu J, Zen K. Kaback HR, et al. J Exp Biol. 1994 Nov;196:183-95. doi: 10.1242/jeb.196.1.183. J Exp Biol. 1994. PMID: 7823021 Review.
The role of helix VIII in the lactose permease of Escherichia coli: I. Cys-scanning mutagenesis.
Frillingos S, Ujwal ML, Sun J, Kaback HR. Frillingos S, et al. Protein Sci. 1997 Feb;6(2):431-7. doi: 10.1002/pro.5560060220. Protein Sci. 1997. PMID: 9041646 Free PMC article.
More direct evidence for the latter conclusion is provided in the companion paper (Frillingos S. Kaback HR, 1997, Protein Sci 6:438-443) by using site-directed sulfhydryl modification of the Cys-replacement mutants in situ....
More direct evidence for the latter conclusion is provided in the companion paper (Frillingos S. Kaback HR, 1997, Protein Sci 6:438-4 …
Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: N-ethylmaleimide-sensitive face of helix II.
Venkatesan P, Liu Z, Hu Y, Kaback HR. Venkatesan P, et al. Biochemistry. 2000 Sep 5;39(35):10649-55. doi: 10.1021/bi0004394. Biochemistry. 2000. PMID: 10978148
Cys-scanning mutagenesis of helix II in the lactose permease of Escherichia coli [Frillingos, S., Sun, J. et al. (1997) Biochemistry 36, 269-273] indicates that one face contains positions where Cys replacement or Cys replacement followed by treatment with N-ethylmaleimide …
Cys-scanning mutagenesis of helix II in the lactose permease of Escherichia coli [Frillingos, S., Sun, J. et al. (1997) Biochemistry …
Fluorescence of native single-Trp mutants in the lactose permease from Escherichia coli: structural properties and evidence for a substrate-induced conformational change.
Weitzman C, Consler TG, Kaback HR. Weitzman C, et al. Protein Sci. 1995 Nov;4(11):2310-8. doi: 10.1002/pro.5560041108. Protein Sci. 1995. PMID: 8563627 Free PMC article.
Overall, the findings are consistent with the proposal (Wu J, Frillingos S, Kaback HR, 1995a, Biochemistry 34:8257-8263) that ligand binding induces a conformational change at the C-terminus of helix I such that Pro 28 and Pro 31, which are on one face, become more accessi …
Overall, the findings are consistent with the proposal (Wu J, Frillingos S, Kaback HR, 1995a, Biochemistry 34:8257-8263) that ligand …
61 results