Protein designProtein design is the rational design of new protein molecules to design novel activity, behavior, or purpose, and to advance basic understanding of protein function. Proteins can be designed from scratch (de novo design) or by making calculated variants of a known protein structure and its sequence (termed protein redesign). Rational protein design approaches make protein-sequence predictions that will fold to specific structures.
Heat shock responseThe heat shock response (HSR) is a cell stress response that increases the number of molecular chaperones to combat the negative effects on proteins caused by stressors such as increased temperatures, oxidative stress, and heavy metals. In a normal cell, proteostasis (protein homeostasis) must be maintained because proteins are the main functional units of the cell. Many proteins take on a defined configuration in a process known as protein folding in order to perform their biological functions.
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.
Limiting magnitudeIn astronomy, limiting magnitude is the faintest apparent magnitude of a celestial body that is detectable or detected by a given instrument. In some cases, limiting magnitude refers to the upper threshold of detection. In more formal uses, limiting magnitude is specified along with the strength of the signal (e.g., "10th magnitude at 20 sigma"). Sometimes limiting magnitude is qualified by the purpose of the instrument (e.g., "10th magnitude for photometry") This statement recognizes that a photometric detector can detect light far fainter than it can reliably measure.
Two-dimensional nuclear magnetic resonance spectroscopyTwo-dimensional nuclear magnetic resonance spectroscopy (2D NMR) is a set of nuclear magnetic resonance spectroscopy (NMR) methods which give data plotted in a space defined by two frequency axes rather than one. Types of 2D NMR include correlation spectroscopy (COSY), J-spectroscopy, exchange spectroscopy (EXSY), and nuclear Overhauser effect spectroscopy (NOESY). Two-dimensional NMR spectra provide more information about a molecule than one-dimensional NMR spectra and are especially useful in determining the structure of a molecule, particularly for molecules that are too complicated to work with using one-dimensional NMR.
First-magnitude starFirst-magnitude stars are the brightest stars in the night sky, with apparent magnitudes lower (i.e. brighter) than +1.50. Hipparchus, in the 1st century BC, introduced the magnitude scale. He allocated the first magnitude to the 20 brightest stars and the sixth magnitude to the faintest stars visible to the naked eye. In the 19th century, this ancient scale of apparent magnitude was logarithmically defined, so that a star of magnitude 1.00 is exactly 100 times as bright as one of 6.00.
Seismic magnitude scalesSeismic magnitude scales are used to describe the overall strength or "size" of an earthquake. These are distinguished from seismic intensity scales that categorize the intensity or severity of ground shaking (quaking) caused by an earthquake at a given location. Magnitudes are usually determined from measurements of an earthquake's seismic waves as recorded on a seismogram. Magnitude scales vary on what aspect of the seismic waves are measured and how they are measured.
IC50DISPLAYTITLE:IC50 Half maximal inhibitory concentration (IC50) is a measure of the potency of a substance in inhibiting a specific biological or biochemical function. IC50 is a quantitative measure that indicates how much of a particular inhibitory substance (e.g. drug) is needed to inhibit, in vitro, a given biological process or biological component by 50%. The biological component could be an enzyme, cell, cell receptor or microorganism. IC50 values are typically expressed as molar concentration.
Chaperone (protein)In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for proteolysis. The first molecular chaperones discovered were a type of assembly chaperones which assist in the assembly of nucleosomes from folded histones and DNA.
Acid dissociation constantIn chemistry, an acid dissociation constant (also known as acidity constant, or acid-ionization constant; denoted K_a) is a quantitative measure of the strength of an acid in solution. It is the equilibrium constant for a chemical reaction HA A^- + H^+ known as dissociation in the context of acid–base reactions. The chemical species HA is an acid that dissociates into , the conjugate base of the acid and a hydrogen ion, .
