Infrared spectroscopyInfrared spectroscopy (IR spectroscopy or vibrational spectroscopy) is the measurement of the interaction of infrared radiation with matter by absorption, emission, or reflection. It is used to study and identify chemical substances or functional groups in solid, liquid, or gaseous forms. It can be used to characterize new materials or identify and verify known and unknown samples. The method or technique of infrared spectroscopy is conducted with an instrument called an infrared spectrometer (or spectrophotometer) which produces an infrared spectrum.
Fourier-transform infrared spectroscopyFourier-transform infrared spectroscopy (FTIR) is a technique used to obtain an infrared spectrum of absorption or emission of a solid, liquid, or gas. An FTIR spectrometer simultaneously collects high-resolution spectral data over a wide spectral range. This confers a significant advantage over a dispersive spectrometer, which measures intensity over a narrow range of wavelengths at a time. The term Fourier-transform infrared spectroscopy originates from the fact that a Fourier transform (a mathematical process) is required to convert the raw data into the actual spectrum.
Fourier-transform spectroscopyFourier-transform spectroscopy is a measurement technique whereby spectra are collected based on measurements of the coherence of a radiative source, using time-domain or space-domain measurements of the radiation, electromagnetic or not. It can be applied to a variety of types of spectroscopy including optical spectroscopy, infrared spectroscopy (FTIR, FT-NIRS), nuclear magnetic resonance (NMR) and magnetic resonance spectroscopic imaging (MRSI), mass spectrometry and electron spin resonance spectroscopy.
Protein–protein interactionProtein–protein interactions (PPIs) are physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by interactions that include electrostatic forces, hydrogen bonding and the hydrophobic effect. Many are physical contacts with molecular associations between chains that occur in a cell or in a living organism in a specific biomolecular context. Proteins rarely act alone as their functions tend to be regulated.
Forensic chemistryForensic chemistry is the application of chemistry and its subfield, forensic toxicology, in a legal setting. A forensic chemist can assist in the identification of unknown materials found at a crime scene. Specialists in this field have a wide array of methods and instruments to help identify unknown substances. These include high-performance liquid chromatography, gas chromatography-mass spectrometry, atomic absorption spectroscopy, Fourier transform infrared spectroscopy, and thin layer chromatography.
Applied spectroscopyApplied spectroscopy is the application of various spectroscopic methods for the detection and identification of different elements or compounds to solve problems in fields like forensics, medicine, the oil industry, atmospheric chemistry, and pharmacology. A common spectroscopic method for analysis is Fourier transform infrared spectroscopy (FTIR), where chemical bonds can be detected through their characteristic infrared absorption frequencies or wavelengths.
Nitrilotriacetic acidNitrilotriacetic acid (NTA) is the aminopolycarboxylic acid with the formula N(CH2CO2H)3. It is a colourless solid that is used as a chelating agent, which forms coordination compounds with metal ions (chelates) such as Ca2+, Co2+, Cu2+, and Fe3+. Nitrilotriacetic acid is commercially available as the free acid and as the sodium salt. It is produced from ammonia, formaldehyde, and sodium cyanide or hydrogen cyanide. Worldwide capacity is estimated at 100 thousand tonnes per year.
Rotational–vibrational spectroscopyRotational–vibrational spectroscopy is a branch of molecular spectroscopy concerned with infrared and Raman spectra of molecules in the gas phase. Transitions involving changes in both vibrational and rotational states can be abbreviated as rovibrational (or ro-vibrational) transitions. When such transitions emit or absorb photons (electromagnetic radiation), the frequency is proportional to the difference in energy levels and can be detected by certain kinds of spectroscopy.
His-tagA polyhistidine-tag, best known by the trademarked name His-tag, is an amino acid motif in proteins that typically consists of at least six histidine (His) residues, often at the N- or C-terminus of the protein. It is also known as a hexa histidine-tag, 6xHis-tag, or His6 tag. The tag was invented by Roche, although the use of histidines and its vectors are distributed by Qiagen. Various purification kits for histidine-tagged proteins are commercially available from multiple companies.
ProteinProteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity.
