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Repressor Proteins
In molecular genetics, a repressor is a DNA- or RNA-binding protein that inhibits the expression of one or more genes by binding to the operator or associated silencers. A DNA-binding repressor blocks the attachment of RNA polymerase to the promoter, thus preventing transcription of the genes into messenger RNA. An RNA-binding repressor binds to the mRNA and prevents translation of the mRNA into protein. This blocking or reducing of expression is called repression. Function If an inducer, a molecule that initiates the gene expression, is present, then it can interact with the repressor protein and detach it from the operator. RNA polymerase then can transcribe the message (expressing the gene). A co-repressor is a molecule that can bind to the repressor and make it bind to the operator tightly, which decreases transcription. A repressor that binds with a co-repressor is termed an ''aporepressor'' or ''inactive repressor''. One type of aporepressor is the trp represso ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glossary Of Gene Expression Terms
A glossary (from , ''glossa''; language, speech, wording), also known as a vocabulary or clavis, is an alphabetical list of terms in a particular domain of knowledge with the definitions for those terms. Traditionally, a glossary appears at the end of a book and includes terms within that book that are either newly introduced, uncommon, or specialized. While glossaries are most commonly associated with non-fiction books, in some cases, fiction novels sometimes include a glossary for unfamiliar terms. A bilingual glossary is a list of terms in one language defined in a second language or glossed by synonyms (or at least near-synonyms) in another language. In a general sense, a glossary contains explanations of concepts relevant to a certain field of study or action. In this sense, the term is related to the notion of ontology. Automatic methods have been also provided that transform a glossary into an ontology or a computational lexicon. Core glossary A ''core glossary' ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Dyad Symmetry
Dyad or dyade may refer to: Arts and entertainment * Dyad (music), a set of two notes or pitches * Dyad (novel), ''Dyad'' (novel), by Michael Brodsky, 1989 * Dyad (video game), ''Dyad'' (video game), 2012 * ''Dyad 1909'' and ''Dyad 1929'', ballets by Wayne McGregor *Dyad Institute, a fictional biotech corporation in the Canadian TV series Orphan Black Other uses * Dyad (biology), a pair of sister chromatids * Dyad (philosophy), used by the Pythagoreans for the number two, representing "twoness" or "otherness" * Dyad (sociology), a group of two people *Grizzled Young Veterans, also known as The Dyad, a British professional wrestling tag team See also * Dyadic (other) * Diad, in cell biology * Dryad (other) * Dyad pedagogy, a goal-directed teaching method * Dyad symmetry, in genetics * Triad (other) ("group of 3") {{disambiguation ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Palindrome
A palindrome (Help:IPA/English, /ˈpæl.ɪn.droʊm/) is a word, palindromic number, number, phrase, or other sequence of symbols that reads the same backwards as forwards, such as ''madam'' or ''racecar'', the date "Twosday, 02/02/2020" and the sentence: "A man, a plan, a canal – Panama". The 19-letter Finnish language, Finnish word ''saippuakivikauppias'' (a soapstone vendor) is the longest single-word palindrome in everyday use, while the 12-letter term ''tattarrattat'' (from James Joyce in ''Ulysses (novel), Ulysses'') is the longest in English. The word ''palindrome'' was introduced by English poet and writer Henry Peacham (born 1578), Henry Peacham in 1638.Henry Peacham, ''The Truth of our Times Revealed out of One Mans Experience'', 1638p. 123 The concept of a palindrome can be dated to the 3rd-century BCE, although no examples survive. The earliest known examples are the 1st-century CE Latin acrostic word square, the Sator Square (which contains both word and senten ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Dimer
In biochemistry, a protein dimer is a macromolecular complex or protein multimer, multimer formed by two protein monomers, or single proteins, which are usually Non-covalent interaction, non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word ''dimer'' has roots meaning "two parts", ''wikt:di-#Prefix, di-'' + ''wikt:-mer#Suffix, -mer''. A protein dimer is a type of protein quaternary structure. A protein homodimer is formed by two identical proteins while a protein heterodimer is formed by two different proteins. Most protein dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer is the enzyme reverse transcriptase, which is composed of two different amino acid chains. An exception is dimers that are linked by disulfide bridges such as the homodimeric protein IKBKG, NEMO. Some proteins contain specialized domains to ensure dimerization (dimerization domains) and specificity. The G protein- ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Beta-sheet
The beta sheet (β-sheet, also β-pleated sheet) is a common structural motif, motif of the regular protein secondary structure. Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone chain, backbone hydrogen bonds, forming a generally twisted, pleated sheet. A β-strand is a stretch of peptide, polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformational isomerism, conformation. The supramolecular association of β-sheets has been implicated in the formation of the Amyloid fibril, fibrils and Amyloid plaques, protein aggregates observed in amyloidosis, Alzheimer's disease and other Proteinopathy, proteinopathies. History The first β-sheet structure was proposed by William Astbury in the 1930s. He proposed the idea of hydrogen bonding between the peptide bonds of parallel or antiparallel extended β-strands. However, Astbury did not have the necessary data on the bond geometry of the amino acids ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Antiparallel (biochemistry)
In biochemistry, two biopolymers are antiparallel if they run parallel (geometry), parallel to each other but with opposite directionality (molecular biology), directionality (alignments). An example is the two complementarity (molecular biology), complementary strands of a DNA nucleic acid double helix, double helix, which antiparallel vectors, run in opposite directions alongside each other. Nucleic acids Nucleic acid molecules have a phosphoryl (5') end and a hydroxyl (3') end. This notation follows from IUPAC nomenclature of organic chemistry, organic chemistry nomenclature, and can be used to define the movement of enzymes such as DNA polymerases relative to the DNA strand in a non-arbitrary manner. G-quadruplexes G-quadruplexes, also known as G4 DNA are secondary structures found in nucleic acids that are rich in guanine. These structures are normally located at the telomeres (the ends of the Chromosome, chromosomes). The G-quadruplex can either be parallel or antiparallel ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha Helix
An 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 Protein secondary structure, 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-handed helix conformation in which every backbone amino, N−H group hydrogen bonds to the backbone carbonyl, C=O group of the amino acid that is four residue (biochemistry), residues earlier in the protein sequence. Other names The alpha helix is also commonly called a: * Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure) * 3.613-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen) Discovery ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Beta Ribbon
The beta sheet (β-sheet, also β-pleated sheet) is a common motif of the regular protein secondary structure. Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet. A β-strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation. The supramolecular association of β-sheets has been implicated in the formation of the fibrils and protein aggregates observed in amyloidosis, Alzheimer's disease and other proteinopathies. History The first β-sheet structure was proposed by William Astbury in the 1930s. He proposed the idea of hydrogen bonding between the peptide bonds of parallel or antiparallel extended β-strands. However, Astbury did not have the necessary data on the bond geometry of the amino acids in order to build accurate models, especially since he did not then know that the peptide bond was planar. A re ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Monomers
A monomer ( ; ''wikt:mono-, mono-'', "one" + ''wikt:-mer, -mer'', "part") is a molecule that can chemical reaction, react together with other monomer molecules to form a larger polymer chain or two- or three-dimensional network in a process called polymerization. Classification Chemistry classifies monomers by type, and two broad classes based on the type of polymer they form. By type: * natural vs synthetic, e.g. glycine vs caprolactam, respectively * polar vs nonpolar, e.g. vinyl acetate vs ethylene, respectively * cyclic vs linear, e.g. ethylene oxide vs ethylene glycol, respectively By type of polymer they form: * those that participate in condensation polymerization * those that participate in addition polymerization Differing stoichiometry causes each class to create its respective form of polymer. : The polymerization of one kind of monomer gives a polymer#Monomers and repeat units, homopolymer. Many polymers are copolymers, meaning that they are derived from two diff ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Homodimer
In biochemistry, a protein dimer is a macromolecular complex or protein multimer, multimer formed by two protein monomers, or single proteins, which are usually Non-covalent interaction, non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word ''dimer'' has roots meaning "two parts", ''wikt:di-#Prefix, di-'' + ''wikt:-mer#Suffix, -mer''. A protein dimer is a type of protein quaternary structure. A protein homodimer is formed by two identical proteins while a protein heterodimer is formed by two different proteins. Most protein dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer is the enzyme reverse transcriptase, which is composed of two different amino acid chains. An exception is dimers that are linked by disulfide bridges such as the homodimeric protein IKBKG, NEMO. Some proteins contain specialized domains to ensure dimerization (dimerization domains) and specificity. The G protein- ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
