Any spectroscopic method based on exciting a sample through resonant or non-resonant interactions with a light
source reaches a detection limit when too few photons interact with the sample. With light scattering techniques
for instance, samples that are deemed too transparent cannot be measured. Solutions around this problem include
means to increase the cross-section of the interactions (absorption, fluorescence, or scattering) using various
probes. While such measurements are widely performed and valid most of the time, this approach can be
problematic if the marker is large enough to perturb the system or introduces possible artifacts. Meanwhile, such
solutions do not break the fundamental limit that the light source most generally travels through - and interact
with - the sample only once.
Here, we propose a technique called Cavity Amplified Scattering Spectroscopy (CASS) that amplifies weak light
scattering signals typically by a factor 103, and thus allows us to study quasi non-scattering objects with no added
probe.
We measured the radius of gyration of highly diluted proteins well beyond the limit of current techniques, and the
spectrum of internal protein motion was obtained over a 9-decades wide frequency domain. Having no complex
sample preparation, and a simple and compact optical setup, CASS represents an attractive complement to other
techniques for the study of internal protein dynamics, and can therefore extend the scope of current light scattering
techniques.