Colligative propertiesIn chemistry, colligative properties are those properties of solutions that depend on the ratio of the number of solute particles to the number of solvent particles in a solution, and not on the nature of the chemical species present.McQuarrie, Donald, et al. Colligative properties of Solutions" General Chemistry Mill Valley: Library of Congress, 2011. . The number ratio can be related to the various units for concentration of a solution such as molarity, molality, normality (chemistry), etc.
Proteinogenic amino acidProteinogenic amino acids are amino acids that are incorporated biosynthetically into proteins during translation. The word "proteinogenic" means "protein creating". Throughout known life, there are 22 genetically encoded (proteinogenic) amino acids, 20 in the standard genetic code and an additional 2 (selenocysteine and pyrrolysine) that can be incorporated by special translation mechanisms.
Gravity waveIn fluid dynamics, gravity waves are waves generated in a fluid medium or at the interface between two media when the force of gravity or buoyancy tries to restore equilibrium. An example of such an interface is that between the atmosphere and the ocean, which gives rise to wind waves. A gravity wave results when fluid is displaced from a position of equilibrium. The restoration of the fluid to equilibrium will produce a movement of the fluid back and forth, called a wave orbit.
Frequency domainIn mathematics, physics, electronics, control systems engineering, and statistics, the frequency domain refers to the analysis of mathematical functions or signals with respect to frequency, rather than time. Put simply, a time-domain graph shows how a signal changes over time, whereas a frequency-domain graph shows how the signal is distributed within different frequency bands over a range of frequencies. A frequency-domain representation consists of both the magnitude and the phase of a set of sinusoids (or other basis waveforms) at the frequency components of the signal.
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.
