Raman spectroscopyRaman spectroscopy (ˈrɑːmən) (named after Indian physicist C. V. Raman) is a spectroscopic technique typically used to determine vibrational modes of molecules, although rotational and other low-frequency modes of systems may also be observed. Raman spectroscopy is commonly used in chemistry to provide a structural fingerprint by which molecules can be identified. Raman spectroscopy relies upon inelastic scattering of photons, known as Raman scattering.
Protein foldingProtein folding is the physical process where a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA into a linear chain of amino acids.
X-ray spectroscopyX-ray spectroscopy is a general term for several spectroscopic techniques for characterization of materials by using x-ray radiation. When an electron from the inner shell of an atom is excited by the energy of a photon, it moves to a higher energy level. When it returns to the low energy level, the energy which it previously gained by the excitation is emitted as a photon which has a wavelength that is characteristic for the element (there could be several characteristic wavelengths per element).
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.
Protein subunitIn structural biology, a protein subunit is a polypeptide chain or single protein molecule that assembles (or "coassembles") with others to form a protein complex. Large assemblies of proteins such as viruses often use a small number of types of protein subunits as building blocks. A subunit is often named with a Greek or Roman letter, and the numbers of this type of subunit in a protein is indicated by a subscript. For example, ATP synthase has a type of subunit called α.
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.
DipoleIn physics, a dipole () is an electromagnetic phenomenon which occurs in two ways: An electric dipole deals with the separation of the positive and negative electric charges found in any electromagnetic system. A simple example of this system is a pair of charges of equal magnitude but opposite sign separated by some typically small distance. (A permanent electric dipole is called an electret.) A magnetic dipole is the closed circulation of an electric current system. A simple example is a single loop of wire with constant current through it.
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.
Protein structureProtein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers - specifically polypeptides - formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond.
Magnetic dipoleIn electromagnetism, a magnetic dipole is the limit of either a closed loop of electric current or a pair of poles as the size of the source is reduced to zero while keeping the magnetic moment constant. It is a magnetic analogue of the electric dipole, but the analogy is not perfect. In particular, a true magnetic monopole, the magnetic analogue of an electric charge, has never been observed in nature. However, magnetic monopole quasiparticles have been observed as emergent properties of certain condensed matter systems.
