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Journal Article

Watching G proteins at work.


Uhl,  R.
Abteilung Neurobiologie, MPI for biophysical chemistry, Max Planck Society;


Wagner,  R.
Abteilung Neurobiologie, MPI for biophysical chemistry, Max Planck Society;


Ryba,  N.
Department of Spectroscopy and Photochemical Kinetics, MPI for biophysical chemistry, Max Planck Society;

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Uhl, R., Wagner, R., & Ryba, N. (1990). Watching G proteins at work. Trends in Neurosciences, 13(2), 64-70. doi:10.1016/0166-2236(90)90070-Q.

Cite as: http://hdl.handle.net/11858/00-001M-0000-0013-0E6C-D
It has been known for over a century that rod photoreceptors in the living retina contract and swell in response to light. Although it is still not known whether this structural light-response is of any functional significance, it has recently been possible to correlate the underlying molecular processes with the activation and deactivation of the photoreceptor G protein, transducin. The technique of light-scattering allows the monitoring of minute changes in cell dimensions, and using this non-invasive experimental approach it can be shown that certain properties of the coupling between transducin and rhodopsin are different in a structurally well-preserved system as compared with rod material used for conventional biochemical studies. Thus, not unlike a psychiatrist, who often learns more about a patient's 'interiors' by observing the body language than by direct interrogation, a biochemist, studying the 'body language' of a cell, may extract information about delicate 'cell interior processes' that would be perturbed by more direct experimental approaches.