J-couplingIn nuclear chemistry and nuclear physics, J-couplings (also called spin-spin coupling or indirect dipole–dipole coupling) are mediated through chemical bonds connecting two spins. It is an indirect interaction between two nuclear spins that arises from hyperfine interactions between the nuclei and local electrons. In NMR spectroscopy, J-coupling contains information about relative bond distances and angles. Most importantly, J-coupling provides information on the connectivity of chemical bonds.
Excimer laserAn excimer laser, sometimes more correctly called an exciplex laser, is a form of ultraviolet laser which is commonly used in the production of microelectronic devices, semiconductor based integrated circuits or "chips", eye surgery, and micromachining. Since 1960s excimer lasers are widely used in high-resolution photolithography machines, one of the critical technologies required for microelectronic chip manufacturing. The term excimer is short for 'excited dimer', while exciplex is short for 'excited complex'.
Laser safetyLaser radiation safety is the safe design, use and implementation of lasers to minimize the risk of laser accidents, especially those involving eye injuries. Since even relatively small amounts of laser light can lead to permanent eye injuries, the sale and usage of lasers is typically subject to government regulations. Moderate and high-power lasers are potentially hazardous because they can burn the retina, or even the skin.
Laser diodeA laser diode (LD, also injection laser diode or ILD, or diode laser) is a semiconductor device similar to a light-emitting diode in which a diode pumped directly with electrical current can create lasing conditions at the diode's junction. Driven by voltage, the doped p–n-transition allows for recombination of an electron with a hole. Due to the drop of the electron from a higher energy level to a lower one, radiation, in the form of an emitted photon is generated. This is spontaneous emission.
Native stateIn biochemistry, the native state of a protein or nucleic acid is its properly folded and/or assembled form, which is operative and functional. The native state of a biomolecule may possess all four levels of biomolecular structure, with the secondary through quaternary structure being formed from weak interactions along the covalently-bonded backbone. This is in contrast to the denatured state, in which these weak interactions are disrupted, leading to the loss of these forms of structure and retaining only the biomolecule's primary structure.
Conformational isomerismIn chemistry, conformational isomerism is a form of stereoisomerism in which the isomers can be interconverted just by rotations about formally single bonds (refer to figure on single bond rotation). While any two arrangements of atoms in a molecule that differ by rotation about single bonds can be referred to as different conformations, conformations that correspond to local minima on the potential energy surface are specifically called conformational isomers or conformers.
Eclipsed conformationIn chemistry an eclipsed conformation is a conformation in which two substituents X and Y on adjacent atoms A, B are in closest proximity, implying that the torsion angle X–A–B–Y is 0°. Such a conformation can exist in any open chain, single chemical bond connecting two sp3-hybridised atoms, and it is normally a conformational energy maximum. This maximum is often explained by steric hindrance, but its origins sometimes actually lie in hyperconjugation (as when the eclipsing interaction is of two hydrogen atoms).
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.
