By irradiating a protein (GFP) with a laser at 397nm, some light is absorbed (for subsequent classical fluorescence), some is transmitted and some is scattered. 1 every 10000000 scattered photons will have a shift in the wavelength, due to experienced vibration and rotations of the interacting GFP. The spectrum of this shifted-light is the Raman spectrum, a GFP fingerprint that, sampled in the femto-second scale, revealed the nuclear dynamics of the wild-type GFP chromophore embedded in the protein beta-barrel structure. (Nature 2009, 462:200).
Using site-directed mutagenesis, a red-emitting mutant (I212L/S463R) of the railroad worm luciferase showed ~8 fold more brightness compared to WT protein and also ~10 fold more stability at 37°C. Interestingly, the half-life of this red-luciferase still remains very short (~10 min), this might be of interest for real-time motion-imaging studies in which reporter accumulation can be detrimental. (Protein Science 2009, Oct 28)
Lego pipettor: bioengineers at Washington university, are presenting at the iGEM2009 a $700 prototypical liquid handling system built from commonly Legos bricks able pipet solution into 96-well plates. (http://2009.igem.org)