If one could attach a fluorescent tag to a macromolecule and then measure its orientation in a cellular environment, then one would have a powerful tool by which to study conformational changes under physiological conditions. Apply this approach to the study of myosin and it should be possible to measure the movement that is thought to drive muscle contraction. This method is not new but until now it has yielded rather ambiguous results because the fluorophores themselves could move independently of the protein to which they were attached. By dint of much hard chemistry, Corrie et al. (Nature 430, 425? 430, 1999) have managed to fix both ends of the bifunctional fluorophore rhodamine to the myosin regulatory light chain (RLC), thereby uniqu...
AbstractTo study the orientation and dynamics of myosin, we measured fluorescence polarization of si...
AbstractFluorescence polarization was used to examine orientation changes of two rhodamine probes bo...
Molecular fluorescence provides scientists with a wealth of information on how biological systems fu...
If one could attach a fluorescent tag to a macromolecule and then measure its orientation in a cellu...
The orientation of the regulatory light chain (RLC) binding region in myosin was investigated by mea...
The orientation of the regulatory light chain (RLC) binding region in myosin was investigated by mea...
The orientation of the light-chain region of myosin heads in relaxed, rigor, and isometrically contr...
The orientation of the light-chain region of myosin heads in relaxed, rigor, and isometrically contr...
The orientation of the light-chain region of myosin heads in relaxed, rigor, and isometrically contr...
AbstractIt is well documented that muscle contraction results from cyclic rotations of actin-bound m...
ABSTRACT The orientation of the light-chain region of myosin heads in relaxed, rigor, and isometrica...
The orientation of the light-chain region of myosin heads in relaxed, rigor, and isometrically contr...
The orientation of the light-chain region of myosin heads in relaxed, rigor, and isometrically contr...
AbstractMyosin head consists of a globular catalytic domain and a long α-helical regulatory domain. ...
ABSTRACT Fluorescence polarization was used to examine orientation changes of two rhodamine probes b...
AbstractTo study the orientation and dynamics of myosin, we measured fluorescence polarization of si...
AbstractFluorescence polarization was used to examine orientation changes of two rhodamine probes bo...
Molecular fluorescence provides scientists with a wealth of information on how biological systems fu...
If one could attach a fluorescent tag to a macromolecule and then measure its orientation in a cellu...
The orientation of the regulatory light chain (RLC) binding region in myosin was investigated by mea...
The orientation of the regulatory light chain (RLC) binding region in myosin was investigated by mea...
The orientation of the light-chain region of myosin heads in relaxed, rigor, and isometrically contr...
The orientation of the light-chain region of myosin heads in relaxed, rigor, and isometrically contr...
The orientation of the light-chain region of myosin heads in relaxed, rigor, and isometrically contr...
AbstractIt is well documented that muscle contraction results from cyclic rotations of actin-bound m...
ABSTRACT The orientation of the light-chain region of myosin heads in relaxed, rigor, and isometrica...
The orientation of the light-chain region of myosin heads in relaxed, rigor, and isometrically contr...
The orientation of the light-chain region of myosin heads in relaxed, rigor, and isometrically contr...
AbstractMyosin head consists of a globular catalytic domain and a long α-helical regulatory domain. ...
ABSTRACT Fluorescence polarization was used to examine orientation changes of two rhodamine probes b...
AbstractTo study the orientation and dynamics of myosin, we measured fluorescence polarization of si...
AbstractFluorescence polarization was used to examine orientation changes of two rhodamine probes bo...
Molecular fluorescence provides scientists with a wealth of information on how biological systems fu...