Identifying Molecules in Infrared
For the first time, researchers can use infrared spectroscopy to determine what type of bonds protein molecules contain and to identify materials. The new technique has been sought to overcome several limitations of the current, standard technique.Image Credit: Hatice Altug, Electrical Engineering Department, Boston University
An interdisciplinary team of researchers has created a new, ultra-sensitive technique to analyze life-sustaining protein molecules. The technique may profoundly change the methodology of biomolecular studies and chart a new path to effective diagnostics and early treatment of complex diseases. Researchers from Boston University and Tufts University near Boston recently demonstrated an infrared spectroscopy technique that can directly identify the "vibrational fingerprints" of extremely small quantities of proteins, the machinery involved in maintaining living organisms. The new technique exploits nanotechnology to overcome several limitations of current, conventional techniques used to study biomolecules. Previous bio-molecular study methods commonly use fluorescence spectroscopy, where biomolecules are labeled with very bright fluorescence tags to track how efficiently they interact with each other. Understanding interactions is important for medical drug research. Molecules consist of atoms bonded to each other with springs. Depending on the mass of atoms, how stiff these springs are, or how the atoms' springs are arranged, the molecules rotate and vibrate at specific frequencies similar to a guitar string that vibrates at specific frequencies depending on the string length. These resonant frequencies are molecule specific and they mostly occur in the infrared frequency range of the electromagnetic spectrum. The sensitivity of infrared spectroscopy previously had been too low to detect these vibrations, particularly from small quantities of samples.
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