Structure-function relationships based on ATP binding and cation occlusion at equilibrium in Na,K-ATPase.

Article

Structure-function relationships based on ATP binding and cation occlusion at equilibrium in Na,K-ATPase.

Acta physiologica Scandinavica. Supplementum - 1 Aug 1998

Jorgensen P L, Nielsen J M, Rasmussen J H, Pedersen P A

Abstract excerpt

This work evaluates the results of measurements of equilibrium binding of ATP and cations in lethal or partially active mutations of Na,K-ATPase that were expressed at high yield in yeast cells. ATP binding studies allowed estimation of the expense in free energy required to position the gamma-ph...

Topics

Adenosine Triphosphate
Amino Acid Sequence
Cations
Molecular Sequence Data
Mutation
Sodium-Potassium-Exchanging ATPase
Structure-Activity Relationship
Yeasts

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