𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Helix proximity and ligand-induced conformational changes in the lactose permease of Escherichia coli determined by site-directed chemical crosslinking

✍ Scribed by Jianhua Wu; H.Ronald Kaback

Book ID
115627991
Publisher
Elsevier Science
Year
1997
Tongue
English
Weight
332 KB
Volume
270
Category
Article
ISSN
0022-2836

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

Ligand-Induced conformational changes in
Ligand-Induced conformational changes in the lactose permease of escherichia coli: Evidence for two binding sites
✍ Jianhua Wu; Stathis Frillingos; John Voss; H. Ronald Kaback πŸ“‚ Article πŸ“… 1994 πŸ› Cold Spring Harbor Laboratory Press 🌐 English βš– 848 KB

## Abstract By using a lactose permease mutant containing a single Cys residue in place of Val 331 (helix X), conformational changes induced by ligand binding were studied. With right‐side‐out membrane vesicles containing Val 331 β†’ Cys permease, lactose transport is inactivated by either __N__‐ethy

A conformational change in the lactose p
A conformational change in the lactose permease of Escherichia coli is induced by ligand binding or membrane potential
✍ Heinrich Jung; Kirsten Jung; H. Ronald Kaback πŸ“‚ Article πŸ“… 1994 πŸ› Cold Spring Harbor Laboratory Press 🌐 English βš– 607 KB

## Abstract Lactose transport in membrane vesicles containing lactose permease with a single Cys residue in place of Val 315 is inactivated by __N__‐ethylmaleimide in a manner that is stimulated by substrate or by a H^+^ electrochemical gradient (δμ, Sahin‐TΓ³th M, Kaback HR, 1993, __Protein Sci 2__