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.
Cell growthCell growth refers to an increase in the total mass of a cell, including both cytoplasmic, nuclear and organelle volume. Cell growth occurs when the overall rate of cellular biosynthesis (production of biomolecules or anabolism) is greater than the overall rate of cellular degradation (the destruction of biomolecules via the proteasome, lysosome or autophagy, or catabolism). Cell growth is not to be confused with cell division or the cell cycle, which are distinct processes that can occur alongside cell growth during the process of cell proliferation, where a cell, known as the mother cell, grows and divides to produce two daughter cells.
Protein tyrosine phosphataseProtein tyrosine phosphatases (EC 3.1.3.48, systematic name protein-tyrosine-phosphate phosphohydrolase) are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins: [a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate Protein tyrosine (pTyr) phosphorylation is a common post-translational modification that can create novel recognition motifs for protein interactions and cellular localization, affect protein stability, and regulate enzyme activity.
Prime omega functionIn number theory, the prime omega functions and count the number of prime factors of a natural number Thereby (little omega) counts each distinct prime factor, whereas the related function (big omega) counts the total number of prime factors of honoring their multiplicity (see arithmetic function). That is, if we have a prime factorization of of the form for distinct primes (), then the respective prime omega functions are given by and . These prime factor counting functions have many important number theoretic relations.
G protein-coupled receptorG protein-coupled receptors (GPCRs), also known as seven-(pass)-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptors, and G protein-linked receptors (GPLR), form a large group of evolutionarily related proteins that are cell surface receptors that detect molecules outside the cell and activate cellular responses. They are coupled with G proteins.
Public-domain-equivalent licensePublic-domain-equivalent license are licenses that grant public-domain-like rights and/or act as waivers. They are used to make copyrighted works usable by anyone without conditions, while avoiding the complexities of attribution or license compatibility that occur with other licenses. No permission or license is required for a work truly in the public domain, such as one with an expired copyright; such a work may be copied at will.
Signal transductionSignal transduction is the process by which a chemical or physical signal is transmitted through a cell as a series of molecular events. Most commonly, protein phosphorylation is catalyzed by protein kinases, ultimately resulting in a cellular response. Proteins responsible for detecting stimuli are generally termed receptors, although in some cases the term sensor is used. The changes elicited by ligand binding (or signal sensing) in a receptor give rise to a biochemical cascade, which is a chain of biochemical events known as a signaling pathway.
Public-domain softwarePublic-domain software is software that has been placed in the public domain, in other words, software for which there is absolutely no ownership such as copyright, trademark, or patent. Software in the public domain can be modified, distributed, or sold even without any attribution by anyone; this is unlike the common case of software under exclusive copyright, where licenses grant limited usage rights.
Soy proteinSoy protein is a protein that is isolated from soybean. It is made from soybean meal that has been dehulled and defatted. Dehulled and defatted soybeans are processed into three kinds of high protein commercial products: soy flour, concentrates, and isolates. Soy protein isolate has been used since 1959 in foods for its functional properties. Soy protein is generally regarded as being concentrated in protein bodies, which are estimated to contain at least 60–70% of the total soybean protein.
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.
Protein dynamicsProteins are generally thought to adopt unique structures determined by their amino acid sequences. However, proteins are not strictly static objects, but rather populate ensembles of (sometimes similar) conformations. Transitions between these states occur on a variety of length scales (tenths of Å to nm) and time scales (ns to s), and have been linked to functionally relevant phenomena such as allosteric signaling and enzyme catalysis.
