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Fluorometric evidence for control of the activity of F1-adenosinetriphosphatase by ligand-induced conformation change

✍ Scribed by Jui H. Wang

Book ID
104921246
Publisher
Springer US
Year
1986
Tongue
English
Weight
553 KB
Volume
18
Category
Article
ISSN
0145-479X

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## 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