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).
Laser pumpingLaser pumping is the act of energy transfer from an external source into the gain medium of a laser. The energy is absorbed in the medium, producing excited states in its atoms. When the number of particles in one excited state exceeds the number of particles in the ground state or a less-excited state, population inversion is achieved. In this condition, the mechanism of stimulated emission can take place and the medium can act as a laser or an optical amplifier. The pump power must be higher than the lasing threshold of the laser.
Laser pointerA laser pointer or laser pen is a small handheld device with a power source (usually a battery) and a laser diode emitting a very narrow coherent low-powered laser beam of visible light, intended to be used to highlight something of interest by illuminating it with a small bright spot of colored light. The small width of the beam and low power of typical laser pointers make the beam itself invisible in a clean atmosphere, only showing a point of light when striking an opaque surface.
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.
Ultrafast laser spectroscopyUltrafast laser spectroscopy is a spectroscopic technique that uses ultrashort pulse lasers for the study of dynamics on extremely short time scales (attoseconds to nanoseconds). Different methods are used to examine the dynamics of charge carriers, atoms, and molecules. Many different procedures have been developed spanning different time scales and photon energy ranges; some common methods are listed below. Dynamics on the as to fs time scale are in general too fast to be measured electronically.
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.
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.
Staggered conformationIn organic chemistry, a staggered conformation is a chemical conformation of an ethane-like moiety abcX–Ydef in which the substituents a, b, and c are at the maximum distance from d, e, and f; this requires the torsion angles to be 60°. It is the opposite of an eclipsed conformation, in which those substituents are as close to each other as possible. Such a conformation exists in any open chain single chemical bond connecting two sp3-hybridised atoms, and is normally a conformational energy minimum.
Laser coolingLaser cooling includes a number of techniques in which atoms, molecules, and small mechanical systems are cooled, often approaching temperatures near absolute zero. Laser cooling techniques rely on the fact that when an object (usually an atom) absorbs and re-emits a photon (a particle of light) its momentum changes. For an ensemble of particles, their thermodynamic temperature is proportional to the variance in their velocity. That is, more homogeneous velocities among particles corresponds to a lower temperature.
Carbon-dioxide laserThe carbon-dioxide laser (CO2 laser) was one of the earliest gas lasers to be developed. It was invented by Kumar Patel of Bell Labs in 1964 and is still one of the most useful types of laser. Carbon-dioxide lasers are the highest-power continuous-wave lasers that are currently available. They are also quite efficient: the ratio of output power to pump power can be as large as 20%. The CO2 laser produces a beam of infrared light with the principal wavelength bands centering on 9.6 and 10.6 micrometers (μm).
Conformational changeProtein dynamics In biochemistry, a conformational change is a change in the shape of a macromolecule, often induced by environmental factors. A macromolecule is usually flexible and dynamic. Its shape can change in response to changes in its environment or other factors; each possible shape is called a conformation, and a transition between them is called a conformational change. Factors that may induce such changes include temperature, pH, voltage, light in chromophores, concentration of ions, phosphorylation, or the binding of a ligand.
Strain (chemistry)In chemistry, a molecule experiences strain when its chemical structure undergoes some stress which raises its internal energy in comparison to a strain-free reference compound. The internal energy of a molecule consists of all the energy stored within it. A strained molecule has an additional amount of internal energy which an unstrained molecule does not. This extra internal energy, or strain energy, can be likened to a compressed spring.
Population inversionIn physics, specifically statistical mechanics, a population inversion occurs while a system (such as a group of atoms or molecules) exists in a state in which more members of the system are in higher, excited states than in lower, unexcited energy states. It is called an "inversion" because in many familiar and commonly encountered physical systems, this is not possible. This concept is of fundamental importance in laser science because the production of a population inversion is a necessary step in the workings of a standard laser.
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.
Alpha helixAn alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the secondary structure of proteins. It is also the most extreme type of local structure, and it is the local structure that is most easily predicted from a sequence of amino acids. The alpha helix has a right hand-helix conformation in which every backbone N−H group hydrogen bonds to the backbone C=O group of the amino acid that is four residues earlier in the protein sequence.
