Use of infra red and magnetic resonance spectroscopy in nano science

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Use of infra red and magnetic resonance spectroscopy in nano science 

Infrared Spectroscopy in Nanotechnology

 Infrared Spectroscopy is one of the widely used well known spectral techniques. This instrument is essential any spectral characterization studies to under the functional groups and crystalline of the long chain molecules. Moreover some of the additional options are available in the latest instruments. For instant, surface analysis and in-situ chemical reactions on substrates and gas phase reactions. Sometime it available in hybrid technique likes TGA with FT-IR to characterize the decomposition products simultaneously.  Microscopic facilities attached FT-IR can be used to identify the surface coating or thin film composition in a submicron diameter scale.

                                    FT-IR is one of the most important techniques to study the binding nature of molecules or capping agent over the nanoparticles surfaces. The main purpose these molecules in nanomaterials to prevent the aggregation of the colloidal particles and used for the functionalization purpose. For the stabilization of metal and metal oxide nanoparticles long chain thiols, amines and carboxylic acids are used. Alternatively polymers, denderimers and clays are also used for the similar kind of applications.

                                    Thus FT-IR instrument is widely used to study the nature of bonding and functional groups present in the nanocomposites. Also some of the surface chemical reaction will be studies with the help of in-situ techniques like ATR-IR and Reflectance IR spectral instruments.

Nuclear magnetic resonance spectroscopy, most commonly known as NMR spectroscopy, is a research technique that exploits the magnetic properties of certain atomic nuclei to determine physical and chemical properties of atoms or the molecules in which they are contained. It relies on the phenomenon of nuclear magnetic resonance and can provide detailed information about the structure, dynamics, reaction state, and chemical environment of molecules.
Nuclear magnetic resonance (NMR) spectroscopy is next to X-ray crystallography the only bio- physical method which can provide high-resolution structures of biological molecules such as proteins and nucleic acids and their complexes at atomic resolution. The first NMR derived three- dimensional solution structure of a small protein was determined in 1985, which means that NMR is about 25 years younger than biomolecular X-ray crystallography
Most frequently, NMR spectroscopy is used by chemists and biochemists to investigate the properties of organic molecules, though it is applicable to any kind of sample that contains nuclei possessing spin. Suitable samples range from small compounds analyzed with 1-dimensional proton or carbon-13 NMR spectroscopy to large proteins or nucleic acids using 3 or 4-dimensional techniques. The impact of NMR spectroscopy on the sciences has been substantial because of the range of information and the diversity of samples, including solutions and solids.