Creative Biolabs offers dual-polarization interferometry (DPI) services, which provide exquisite sensitivity to give previously unavailable insights into the structural changes taking place in molecular systems as they function and interact. DPI resolves protein structure to subatomic dimensions in real time and is typically used to characterize biochemical interactions by quantifying any conformational change at the same time as measuring reaction rates, affinities and thermodynamics.
DPI measures the structure of a protein in one dimension (i.e. its diameter or size) and the density (i.e. its mass per unit volume or how tightly folded it is) by coupling the protein to a glass slide and probing its structure using non-diffractive optics. DPI offers the ability to quantify changes in the thickness and density on the chip surface, shape orientation, binding & conformational changes, membrane behavior and interactions, etc.
Data generated from our DPI quantitative structural measurements can be compared directly with complimentary techniques such as X-ray crystallography, NMR and neutron reflection, whilst also being capable of functional measurement at far higher sensitivity and with less ambiguity than classical optical and acoustic biosensor technologies.