Independent flexible motion of submolecular domains of the calcium-magnesium ATPase of sarcoplasmic reticulum measured by time-resolved fluorescence depolarization of site-specifically attached probes
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00445a032
Reference37 articles.
1. Chemical Modification and Fluorescence Labeling Study of Ca2+,Mg2+-Adenosine Triphosphatase of Sarcoplasmic Reticulum Using lodoacetamide and Its N-Substituted Derivatives1
2. Similarity of the Active Site of Phosphorylation of the Adenosine Triphosphatase for Transport of Sodium and Potassium Ions in Kidney to That for Transport of Calcium Ions in the Sarcoplasmic Reticulum of Muscle
3. Time-resolved x-ray diffraction studies of the sarcoplasmic reticulum membrane during active transport
4. Two Ca2+ ATPase genes: Homologies and mechanistic implications of deduced amino acid sequences
5. Rotation motion and flexibility of calcium(2+),magnesium(2+)-dependent adenosine 5'-triphosphatase in sarcoplasmic reticulum membranes
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