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.
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.
Public domainThe public domain (PD) consists of all the creative work to which no exclusive intellectual property rights apply. Those rights may have expired, been forfeited, expressly waived, or may be inapplicable. Because no one holds the exclusive rights, anyone can legally use or reference those works without permission. As examples, the works of William Shakespeare, Ludwig van Beethoven, Leonardo da Vinci and Georges Méliès are in the public domain either by virtue of their having been created before copyright existed, or by their copyright term having expired.
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.
Weierstrass elliptic functionIn mathematics, the Weierstrass elliptic functions are elliptic functions that take a particularly simple form. They are named for Karl Weierstrass. This class of functions are also referred to as ℘-functions and they are usually denoted by the symbol ℘, a uniquely fancy script p. They play an important role in the theory of elliptic functions. A ℘-function together with its derivative can be used to parameterize elliptic curves and they generate the field of elliptic functions with respect to a given period lattice.
Domain nameIn the Internet, a domain name is a string that identifies a realm of administrative autonomy, authority or control. Domain names are often used to identify services provided through the Internet, such as websites, email services and more. As of 2017, 330.6 million domain names had been registered. Domain names are used in various networking contexts and for application-specific naming and addressing purposes. In general, a domain name identifies a network domain or an Internet Protocol (IP) resource, such as a personal computer used to access the Internet, or a server computer.
Heat shock proteinHeat shock proteins (HSP) are a family of proteins produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock, but are now known to also be expressed during other stresses including exposure to cold, UV light and during wound healing or tissue remodeling. Many members of this group perform chaperone functions by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress.
Lemniscate elliptic functionsIn mathematics, the lemniscate elliptic functions are elliptic functions related to the arc length of the lemniscate of Bernoulli. They were first studied by Giulio Fagnano in 1718 and later by Leonhard Euler and Carl Friedrich Gauss, among others. The lemniscate sine and lemniscate cosine functions, usually written with the symbols sl and cl (sometimes the symbols sinlem and coslem or sin lemn and cos lemn are used instead), are analogous to the trigonometric functions sine and cosine.
Protein superfamilyA protein superfamily is the largest grouping (clade) of proteins for which common ancestry can be inferred (see homology). Usually this common ancestry is inferred from structural alignment and mechanistic similarity, even if no sequence similarity is evident. Sequence homology can then be deduced even if not apparent (due to low sequence similarity). Superfamilies typically contain several protein families which show sequence similarity within each family.
Arithmetic functionIn number theory, an arithmetic, arithmetical, or number-theoretic function is for most authors any function f(n) whose domain is the positive integers and whose range is a subset of the complex numbers. Hardy & Wright include in their definition the requirement that an arithmetical function "expresses some arithmetical property of n". An example of an arithmetic function is the divisor function whose value at a positive integer n is equal to the number of divisors of n.
