Infrared sheds light on single protein complexes

Researchers from the nanoscience research center CIC nanoGUNE, the Freie Universität Berlin and Neaspec company employ nano-FTIR spectroscopy for label-free chemical and structural imaging of proteins with nanoscale spatial resolution and with sensitivity to single protein complexes of less than…

Researchers from the nanoscience research center CIC nanoGUNE, the Freie Universität Berlin and Neaspec company employ nano-FTIR spectroscopy for label-free chemical and structural imaging of proteins with nanoscale spatial resolution and with sensitivity to single protein complexes of less than one attogram (10-18 gram). The work has been published recently in Nature Communications.

Proteins are basic building blocks of life. The chemistry and structure of proteins are essential for their biological function. Indeed, the structure of proteins determines their mechanical and catalytic properties (e.g. enzymes). Such functions literally shape all living beings. Furthermore, the protein structure also plays a major role in many diseases. For example, the secondary structure of a protein (whether it has helical (alpha-) or sheet-like (beta-) internal substructures) is highly relevant in the pathogenous mechanism leading to Alzheimer, Parkinson, and other neuro-degenerative diseases. Although a variety of methods have been developed to study the protein chemistry and structure, recognizing and mapping the secondary structure on the nanometer scale, or even with single protein sensitivity, is still a major challenge. A new infrared spectroscopy technique, called nano-FTIR, has now enabled nanoscale chemical imaging and probing of protein’s secondary structure with enormous sensitivity.

Read more at: http://phys.org/news/2013-12-infrared-protein-complexes.html#jCp