From structure to cellular mechanism with infrared microspectroscopy.
Summary of "From structure to cellular mechanism with infrared microspectroscopy."
Current efforts in structural biology aim to integrate structural information within the context of cellular organization and function. X-rays and infrared radiation stand at opposite ends of the electromagnetic spectrum and act as complementary probes for achieving this goal. Intense and bright beams are produced by synchrotron radiation, and are efficiently used in the wavelength domain extending from hard X-rays to the far-infrared (or THz) regime. While X-ray crystallography provides exquisite details on atomic structure, Fourier transform infrared microspectroscopy (FTIRM) is emerging as a spectroscopic probe and imaging tool for correlating molecular structure to biochemical dynamics and function. In this manuscript, the role of synchrotron FTIRM in bridging the gap towards 'functional biology' is discussed based upon recent achievements, with a critical assessment of the contributions to biological and biomedical research.
Affiliation
National Synchrotron Light Source, Brookhaven National Laboratory, Upton, NY, USA.
Journal Details
This article was published in the following journal.
Name: Current opinion in structural biology
ISSN: 1879-033X
Pages:
Links
- PubMed Source: http://www.ncbi.nlm.nih.gov/pubmed/20739176
- DOI: http://dx.doi.org/10.1016/j.sbi.2010.07.007
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Measurement of the regional temperature of the body or an organ by infrared sensing devices, based on self-emanating infrared radiation.
Infrared Rays
That portion of the electromagnetic spectrum usually sensed as heat. Infrared wavelengths are longer than those of visible light, extending into the microwave frequencies. They are used therapeutically as heat, and also to warm food in restaurants.
Spectrophotometry, Infrared
Spectrophotometry in the infrared region, usually for the purpose of chemical analysis through measurement of absorption spectra associated with rotational and vibrational energy levels of molecules. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
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Decorin
A small leucine-rich proteoglycan that interacts with FIBRILLAR COLLAGENS and modifies the EXTRACELLULAR MATRIX structure of CONNECTIVE TISSUE. Decorin has also been shown to play additional roles in the regulation of cellular responses to GROWTH FACTORS. The protein contains a single glycosaminoglycan chain and is similar in structure to BIGLYCAN.
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