ABSTRACT: We have studied the effects of vanadate on the rotational motion of the calcium adenosine-triphosphatase (Ca-ATPase) from sarcoplasmic reticulum (SR), using saturation-transfer electron para-magnetic resonance (ST-EPR). Vanadate has been proposed to act as a phosphate analogue and produce a stable intermediate state similar to the phosphoenzyme. This study provides evidence about the physical state of this intermediate. In particular, since ST-EPR provides a sensitive measure of microsecond protein rotational mobility, and hence of protein-protein association, these studies allowed us to ask (a) whether the vanadate-induced protein association observed in electron micrographs of S R vesicles also occurs unde
ABSTRACT: We have used time-resolved phosphorescence anisotropy and electron paramagnetic resonance ...
Vanadate is the hallmark inhibitor of the P-type ATPase family; however, structural details of its i...
Inorg Chem. 2008 Jul 7;47(13):5677-84. doi: 10.1021/ic702405dThe general affinity of the sarcoplasmi...
Vanadate binding to sarcoplasmic reticulum vesicles results in the loss of the externally located hi...
ABSTRACT: We have used frequency- and time-resolved electron paramagnetic resonance (EPR) to study t...
Although not stable, once formed, decameric vanadate (V10) disintegration is in general slow enough ...
Vanadate binding to different sarcoplasmic reticulum membrane preparations was determined by measuri...
Lipid deprivation of the sarcoplasmic reticulum calcium‐transport ATPase neither affects the enzyme'...
The technique of saturation transfer electron spin resonance has been applied to study the rotationa...
The affinity of the sarcoplasmic reticulum transport ATPase for calcium and ATP is not affected by l...
AbstractSarcoplasmic reticulum vesicles were incubated with the maleimide-directed probe ThioGlo1, r...
Vanadate is the hallmark inhibitor of the P-type ATPase family; however, structural details of its i...
The calcium free sarcoplasmic reticulum calcium transport ATPase incorporates in the presence of mag...
ABSTRACT: We have studied the effect of phospholipid chain length on the activity and molecular dyna...
The general affinity of the sarcoplasmic reticulum (SR) Ca2+-ATPase was examined for three different...
ABSTRACT: We have used time-resolved phosphorescence anisotropy and electron paramagnetic resonance ...
Vanadate is the hallmark inhibitor of the P-type ATPase family; however, structural details of its i...
Inorg Chem. 2008 Jul 7;47(13):5677-84. doi: 10.1021/ic702405dThe general affinity of the sarcoplasmi...
Vanadate binding to sarcoplasmic reticulum vesicles results in the loss of the externally located hi...
ABSTRACT: We have used frequency- and time-resolved electron paramagnetic resonance (EPR) to study t...
Although not stable, once formed, decameric vanadate (V10) disintegration is in general slow enough ...
Vanadate binding to different sarcoplasmic reticulum membrane preparations was determined by measuri...
Lipid deprivation of the sarcoplasmic reticulum calcium‐transport ATPase neither affects the enzyme'...
The technique of saturation transfer electron spin resonance has been applied to study the rotationa...
The affinity of the sarcoplasmic reticulum transport ATPase for calcium and ATP is not affected by l...
AbstractSarcoplasmic reticulum vesicles were incubated with the maleimide-directed probe ThioGlo1, r...
Vanadate is the hallmark inhibitor of the P-type ATPase family; however, structural details of its i...
The calcium free sarcoplasmic reticulum calcium transport ATPase incorporates in the presence of mag...
ABSTRACT: We have studied the effect of phospholipid chain length on the activity and molecular dyna...
The general affinity of the sarcoplasmic reticulum (SR) Ca2+-ATPase was examined for three different...
ABSTRACT: We have used time-resolved phosphorescence anisotropy and electron paramagnetic resonance ...
Vanadate is the hallmark inhibitor of the P-type ATPase family; however, structural details of its i...
Inorg Chem. 2008 Jul 7;47(13):5677-84. doi: 10.1021/ic702405dThe general affinity of the sarcoplasmi...