<p>A: Binding of Ca<sup>2+</sup> with CaM. The backward rate constants of Ca<sup>2+</sup> with CaM are changed in the presence of CNG channels (red). B: Binding of cAMP (gray) with the CNG channels. C: The model of interaction between CNG channels and Ca<sup>2+</sup>/CaM considered that CNG channels can associate to CaM with less than four Ca<sup>2+</sup>. However, the interaction between CNG channels and CaM with one or two Ca<sup>2+</sup> has a weaker affinity than the interaction between CNG channels and CaM with three or four Ca<sup>2+</sup>. Ca<sup>2+</sup>/CaM can bind to open and closed CNG channels with the same affinities. D: Binding of Ca<sup>2+</sup> to CAC channels.</p
“Single-channel” rates are reciprocals of closed times (B), or the reciprocal of the open time minus...
Mediate conformations. The differences in the amount of bound ligand allow quantification of the deg...
<p>Rates were either obtained from the biochemical measurements, adjusted (adj) to reproduce other d...
<p>(A) Ca<sup>2+</sup> binds to a CaM molecule that already has 3 Ca<sup>2+</sup> bound, making the ...
Occupied site is assumed to influence and increase the affinity of the second site. The second site,...
Occupied site is assumed to influence and increase the affinity of the second site. The second site,...
Cyclic nucleotide-gated (CNG) channels have a key role in the conversion of sensory information, suc...
Rythrocyte CaCaATPase, skeletal Myosin Light Chain Kinase (skMLCK) (A). (B) and (C) show the Cabindi...
<p>(A) With 3× Ca<sup>2+</sup> influx, phosphorylated CaMKII subunits in the presence of 5 Hz (blue)...
Ediate conformations. The differences in the amount of bound ligand allow quantification of the degr...
During the acquisition of memories, influx of Ca2+ into the postsynaptic spine through the pores of ...
AbstractcAMP and cGMP differentially bind to and regulate a variety of proteins, including cyclic nu...
<p>Each lobe has two binding sites for calcium, two possible conformations, and can bind targets wit...
The ability of Ca ions to inhibit Ca channels presents one of the most intriguing problems in membra...
AbstractActive Ca2+/calmodulin (CaM)-dependent myosin light chain kinase (MLCK) plays an important r...
“Single-channel” rates are reciprocals of closed times (B), or the reciprocal of the open time minus...
Mediate conformations. The differences in the amount of bound ligand allow quantification of the deg...
<p>Rates were either obtained from the biochemical measurements, adjusted (adj) to reproduce other d...
<p>(A) Ca<sup>2+</sup> binds to a CaM molecule that already has 3 Ca<sup>2+</sup> bound, making the ...
Occupied site is assumed to influence and increase the affinity of the second site. The second site,...
Occupied site is assumed to influence and increase the affinity of the second site. The second site,...
Cyclic nucleotide-gated (CNG) channels have a key role in the conversion of sensory information, suc...
Rythrocyte CaCaATPase, skeletal Myosin Light Chain Kinase (skMLCK) (A). (B) and (C) show the Cabindi...
<p>(A) With 3× Ca<sup>2+</sup> influx, phosphorylated CaMKII subunits in the presence of 5 Hz (blue)...
Ediate conformations. The differences in the amount of bound ligand allow quantification of the degr...
During the acquisition of memories, influx of Ca2+ into the postsynaptic spine through the pores of ...
AbstractcAMP and cGMP differentially bind to and regulate a variety of proteins, including cyclic nu...
<p>Each lobe has two binding sites for calcium, two possible conformations, and can bind targets wit...
The ability of Ca ions to inhibit Ca channels presents one of the most intriguing problems in membra...
AbstractActive Ca2+/calmodulin (CaM)-dependent myosin light chain kinase (MLCK) plays an important r...
“Single-channel” rates are reciprocals of closed times (B), or the reciprocal of the open time minus...
Mediate conformations. The differences in the amount of bound ligand allow quantification of the deg...
<p>Rates were either obtained from the biochemical measurements, adjusted (adj) to reproduce other d...