Location of high-affinity metal binding sites in the profile structure of the Ca+2-ATPase in the sarcoplasmic reticulum by resonance x-ray diffraction.

Lignende værker

• Changes in the relative occupancy of metal-binding sites in the profile structure of the sarcoplasmic reticulum membrane induced by phosphorylation of the Ca2+ATPase enzyme in the presence of terbium: a time-resolved, resonance x-ray diffraction study.
  af: Asturias, F J, et al.
  Udgivet: (1994)
• Changes in the profile structure of the sarcoplasmic reticulum membrane induced by phosphorylation of the Ca2+ ATPase enzyme in the presence of terbium: a time-resolved x-ray diffraction study.
  af: Asturias, F J, et al.
  Udgivet: (1994)
• Effect of Ca2+ binding on the profile structure of the sarcoplasmic reticulum membrane using time-resolved x-ray diffraction.
  af: DeLong, L. J., et al.
  Udgivet: (1993)
• Time-resolved x-ray diffraction studies of the sarcoplasmic reticulum membrane during active transport.
  af: Blasie, J K, et al.
  Udgivet: (1985)
• Evidence that lipid lateral phase separation induces functionally significant structural changes in the Ca+2ATPase of the sarcoplasmic reticulum.
  af: Asturias, F J, et al.
  Udgivet: (1990)