December 9, 1980Biochemistry
Proton nuclear magnetic resonance and electron paramagnetic resonance studies on skeletal muscle actin indicate that the metal and nucleotide binding sites are separate
Population
Skeletal muscle actin (G-actin and F-actin)
Comparison
Replacement of bound Ca2+ or Mg2+ with trivalent… vs Diamagnetic La3+ control (for NMR experiments)
Design
Preclinical
Authors
Discussion
Loading...
Member takes
Implication
No clinical implications for actinopathies; leaves open functional consequences of site separation in muscle.
Structured PICO
P
Population
Skeletal muscle actin (G-actin and F-actin)
I
Intervention
Replacement of bound Ca2+ or Mg2+ with trivalent lanthanide ions (La3+, Eu3+, Gd3+) or use of an ATP analogue with a nitroxide spin-label and Mn2+
C
Comparator
Diamagnetic La3+ control (for NMR experiments)
O
Outcome
Distance separating the high-affinity binding sites of actin for a divalent metal ion and nucleotide
This basic science study demonstrates that the cation and nucleotide binding sites on skeletal muscle actin are physically separated by at least 16 A, rather than forming a complex.
Cite This Study
Barden et al. (1980) studied this question.