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c_hvil6p92t2f5 | In molecular biology, a downstream promoter element (DPE) is a core promoter element. Like all core promoters, the DPE plays an important role in the initiation of gene transcription by RNA polymerase II. The DPE was first described by T. W. Burke and James T. Kadonaga in Drosophila melanogaster at the University of Ca... | Downstream promoter element |
c_e95jd21hxdi2 | It is also present in other species including humans, but not Saccharomyces cerevisiae.Together with the initiator motif (Inr), another core promoter element, the DPE is recognized by the transcription factor II D (TFIID) subunits TAF6 and TAF9. It has been shown that DPE-dependent basal transcription depends highly on... | Downstream promoter element |
c_v0i86r9aw901 | In molecular biology, a guanine tetrad (also known as a G-tetrad or G-quartet) is a structure composed of four guanine bases in a square planar array. They most prominently contribute to the structure of G-quadruplexes, where their hydrogen bonding stabilizes the structure. Usually, there are at least two guanine tetra... | Guanine tetrad |
c_s2aijxxoywwy | They may also play a role in the dimerization of non-endogenous RNAs to facilitate the replication of some viruses. Guanine tetrads dimerize through their 5' ends since it is more energetically favorable.They can be stabilized by central cations, such as lithium, sodium, potassium, rubidium, or cesium. However, they st... | Guanine tetrad |
c_nz1r5tu6uc03 | Guanine tetrads are not always stable, but the sugar-phosphate backbone of DNA can assist in stability of the guanine tetrads themselves. Guanine tetrads are more stable when stacked, as intermolecular forces between each layers help stabilize them.Guanine tetrads can also influence recombination, replication, and tran... | Guanine tetrad |
c_ty58jj4jw6q7 | In molecular biology, a histone octamer is the eight-protein complex found at the center of a nucleosome core particle. It consists of two copies of each of the four core histone proteins (H2A, H2B, H3, and H4). The octamer assembles when a tetramer, containing two copies of H3 and two of H4, complexes with two H2A/H2B... | Histone octamer |
c_fqdw7krq4qbw | In molecular biology, a hybridization probe (HP) is a fragment of DNA or RNA of usually 15–10000 nucleotide long which can be radioactively or fluorescently labeled. HP can be used to detect the presence of nucleotide sequences in analyzed RNA or DNA that are complementary to the sequence in the probe. The labeled prob... | Radioactive probes |
c_io9znes2kedv | Commonly used markers are 32P (a radioactive isotope of phosphorus incorporated into the phosphodiester bond in the probe DNA), digoxigenin, a non-radioactive, antibody-based marker, biotin or fluorescein. DNA sequences or RNA transcripts that have moderate to high sequence similarity to the probe are then detected by ... | Radioactive probes |
c_royk2q0is5rv | Detection of sequences with moderate or high similarity depends on how stringent the hybridization conditions were applied—high stringency, such as high hybridization temperature and low salt in hybridization buffers, permits only hybridization between nucleic acid sequences that are highly similar, whereas low stringe... | Radioactive probes |
c_an8zd0wlkqyu | In order to increase the in vivo stability of the probe RNA is not used. Instead, RNA analogues may be used, in particular morpholino- derivatives. Molecular DNA- or RNA-based probes are routinely used in screening gene libraries, detecting nucleotide sequences with blotting methods, and in other gene technologies, suc... | Radioactive probes |
c_8g3dn1ikdnvs | In molecular biology, a library is a collection of DNA fragments that is stored and propagated in a population of micro-organisms through the process of molecular cloning. There are different types of DNA libraries, including cDNA libraries (formed from reverse-transcribed RNA), genomic libraries (formed from genomic D... | Library (biology) |
c_yxhzeq2a41p0 | In molecular biology, a phage major coat protein is an alpha-helical protein that forms a viral envelope of filamentous bacteriophages. These bacteriophages are flexible rods, about one to two micrometres long and six nm in diameter, with a helical shell of protein subunits surrounding a DNA core. The approximately 50-... | Phage major coat protein |
c_5wwxfnuur0m1 | In molecular biology, a polynucleotide (from Ancient Greek πολυς (polys) 'many') is a biopolymer composed of 13 nucleotide monomers, covalently bonded in a chain. DNA (deoxyribonucleic acid) and RNA (ribonucleic acid) are examples of polynucleotides with distinct biological functions. DNA consists of two chains of poly... | Polynucleotide |
c_sgdota6v8emz | In molecular biology, a primosome is a protein complex responsible for creating RNA primers on single stranded DNA during DNA replication. The primosome consists of seven proteins: DnaG primase, DnaB helicase, DnaC helicase assistant, DnaT, PriA, Pri B, and PriC. At each replication fork, the primosome is utilized once... | Primosome |
c_51a48eetrii7 | Then the DnaB-DnaC helicase complex attaches along with DnaT. This structure is referred to as the pre-primosome. Finally, DnaG will bind to the pre-primosome forming a complete primosome. | Primosome |
c_1ygavade1a9a | The primosome attaches 1-10 RNA nucleotides to the single stranded DNA creating a DNA-RNA hybrid. This sequence of RNA is used as a primer to initiate DNA polymerase III. The RNA bases are ultimately replaced with DNA bases by RNase H nuclease (eukaryotes) or DNA polymerase I nuclease (prokaryotes). | Primosome |
c_dw99d9b028l7 | DNA Ligase then acts to join the two ends together. Assembly of the Escherichia coli primosome requires six proteins, PriA, PriB, PriC, DnaB, DnaC, and DnaT, acting at a primosome assembly site (pas) on an SSBcoated single-stranded (8s) DNA. Assembly is initiated by interactions of PriA and PriB with ssDNA and the pas. | Primosome |
c_6tburfy817h1 | PriC, DnaB, DnaC, and DnaT then act on the PriAPriB- DNA complex to yield the primosome.Primosomes are nucleoproteins assemblies that activate DNA replication forks. Their primary role is to recruit the replicative helicase onto single-stranded DNA. The "replication restart" primosome, defined in Escherichia coli, is i... | Primosome |
c_htiggbmncpot | Binding of the PriA protein to forked DNA triggers its assembly. PriA is conserved in bacteria, but its primosomal partners are not. In Bacillus subtilis, genetic analysis has revealed three primosomal proteins, DnaB, DnaD, and DnaI, that have no obvious homologues in E. coli. | Primosome |
c_d6cdint46tt0 | They are involved in primosome function both at arrested replication forks and at the chromosomal origin. Our biochemical analysis of the DnaB and DnaD proteins unravels their role in primosome assembly. They are both multimeric and bind individually to DNA. | Primosome |
c_yji2fp0ujqgw | Furthermore, DnaD stimulates DnaB binding activities. DnaD alone and the DnaD/DnaB pair interact specifically with PriA of B. subtilis on several DNA substrates. | Primosome |
c_27s6nnb02n3b | This suggests that the nucleoprotein assembly is sequential in the PriA, DnaD, DnaB order. The preferred DNA substrate mimics an arrested DNA replication fork with unreplicated lagging strand, structurally identical to a product of recombinational repair of a stalled replication fork. == References == | Primosome |
c_8hsd8assh3kg | In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. | Protein domain |
c_0az4g10v3ghv | Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal... | Protein domain |
c_6492xatdkf3e | In molecular biology, a reading frame is a way of dividing the sequence of nucleotides in a nucleic acid (DNA or RNA) molecule into a set of consecutive, non-overlapping triplets. Where these triplets equate to amino acids or stop signals during translation, they are called codons. A single strand of a nucleic acid mol... | Reading frame |
c_54l25ggikcym | There are three reading frames that can be read in this 5′→3′ direction, each beginning from a different nucleotide in a triplet. In a double stranded nucleic acid, an additional three reading frames may be read from the other, complementary strand in the 5′→3′ direction along this strand. As the two strands of a doubl... | Reading frame |
c_4zshy4cgx736 | In molecular biology, a reporter gene (often simply reporter) is a gene that researchers attach to a regulatory sequence of another gene of interest in bacteria, cell culture, animals or plants. Such genes are called reporters because the characteristics they confer on organisms expressing them are easily identified an... | Reporter gene |
c_dawgsffke5cz | In molecular biology, a scissile bond is a covalent chemical bond that can be broken by an enzyme. Examples would be the cleaved bond in the self-cleaving hammerhead ribozyme or the peptide bond of a substrate cleaved by a peptidase. == References == | Scissile bond |
c_ayfuyn1r1k9x | In molecular biology, a termination factor is a protein that mediates the termination of RNA transcription by recognizing a transcription terminator and causing the release of the newly made mRNA. This is part of the process that regulates the transcription of RNA to preserve gene expression integrity and are present i... | Termination factor |
c_9qlh7xi8s2l1 | In molecular biology, a transcription factor (TF) (or sequence-specific DNA-binding factor) is a protein that controls the rate of transcription of genetic information from DNA to messenger RNA, by binding to a specific DNA sequence. The function of TFs is to regulate—turn on and off—genes in order to make sure that th... | Transcription factor |
c_xz0ygxbg69eu | Transcription factors are members of the proteome as well as regulome. TFs work alone or with other proteins in a complex, by promoting (as an activator), or blocking (as a repressor) the recruitment of RNA polymerase (the enzyme that performs the transcription of genetic information from DNA to RNA) to specific genes.... | Transcription factor |
c_v6q88io5tjqp | In molecular biology, a twintron is an intron-within-intron excised by sequential splicing reactions. A twintron is presumably formed by the insertion of a mobile intron into an existing intron. | Twintron |
c_zw4fyqfqwods | In molecular biology, acetate kinase (EC 2.7.2.1), which is predominantly found in micro-organisms, facilitates the production of acetyl-CoA by phosphorylating acetate in the presence of ATP and a divalent cation. Short-chain fatty acids (SCFAs) play a major role in carbon cycle and can be utilized as a source of carbo... | Acetate kinase |
c_zgss3l8gz2x0 | Inhibition of StTdcD by tricarboxylic acid (TCA) cycle intermediates such as citrate, succinate, α-ketoglutarate and malate suggests that the enzyme could be under plausible feedback regulation. Crystal structures of StTdcD bound to PO4 (phosphate), AMP, ATP, Ap4 (adenosine tetraphosphate), GMP, GDP, GTP, CMP and CTP r... | Acetate kinase |
c_zex0r9ymwix2 | Molecular dynamics simulations on monomeric and dimeric forms of StTdcD revealed plausible open and closed states, and also suggested role for dimerization in stabilizing segment 235-290 involved in interfacial interactions and ligand binding. Observation of an ethylene glycol molecule bound sufficiently close to the γ... | Acetate kinase |
c_atb50mtq73wu | The growth of a bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme is involved in excretion of excess carbohydrate. A related enzyme, butyrate kinase, facilitates the formation of butyryl-CoA by phosphorylating butyrate in the presence of ATP to form butyryl ph... | Acetate kinase |
c_kvocw10u45gw | In molecular biology, adenylosuccinate synthase (or adenylosuccinate synthetase) (EC 6.3.4.4) is an enzyme that plays an important role in purine biosynthesis, by catalysing the guanosine triphosphate (GTP)-dependent conversion of inosine monophosphate (IMP) and aspartic acid to guanosine diphosphate (GDP), phosphate a... | Adenylosuccinate synthetase |
c_3l4y9yzp1ttc | In molecular biology, aerolysin is a cytolytic pore-forming toxin exported by Aeromonas hydrophila, a Gram-negative bacterium associated with diarrhoeal diseases and deep wound infections. The mature toxin binds to eukaryotic cells and aggregates to form holes (approximately 3 nm in diameter) leading to the destruction... | Aerolysin |
c_x9ws1vnfhakp | In molecular biology, alanine scanning is a site-directed mutagenesis technique used to determine the contribution of a specific residue to the stability or function of a given protein. Alanine is used because of its non-bulky, chemically inert, methyl functional group that nevertheless mimics the secondary structure p... | Alanine scanning |
c_v4d7x8cxrxqs | This is usually accomplished by site-directed mutagenesis or randomly by creating a PCR library. Furthermore, computational methods to estimate thermodynamic parameters based on theoretical alanine substitutions have been developed. This technique is rapid, because many side chains are analyzed simultaneously and the n... | Alanine scanning |
c_yjjbm41vljuz | The technology is very mature at this point and is widely used in biochemical fields. The data can be tested by IR, NMR Spectroscopy, mathematical methods, bioassays, etc.One good example of alanine scanning is the examination of the role of charged residues on the surface of proteins. In a systematic study on the role... | Alanine scanning |
c_8l47923ay02s | In molecular biology, alpha-amylase inhibitor (or α-...) is a protein family which inhibits mammalian alpha-amylases specifically, by forming a tight stoichiometric 1:1 complex with alpha-amylase. This family of inhibitors has no action on plant and microbial alpha amylases. A crystal structure has been determined for ... | Alpha amylase inhibitor |
c_6i3a2kyosqz4 | The crystal structure of tendamistat revealed an immunoglobulin-like fold that could potentially adopt multiple conformations. Such molecular flexibility could enable an induced-fit type of binding that would both optimise binding and allow broad target specificity. == References == | Alpha amylase inhibitor |
c_b7lvbdock2ay | In molecular biology, an Anfinsen cage is a model for protein folding used by some cells to improve the production speed and yield of accurate products. Space within a cell is generally limited, and a protein's folding process can be interrupted or modified if it wanders too close to outside forces while it is still in... | Anfinsen cage |
c_u06gtmg878ax | These cages can also serve to isolate incorrectly formed proteins that may otherwise affect other processes if it were allowed to float freely. The model is named after Christian B. Anfinsen who first showed in vitro that pure denatured proteins will sometimes refold spontaneously without an energy source. == Reference... | Anfinsen cage |
c_9pr6uq6g4hwg | In molecular biology, an actomyosin contractile ring is a prominent structure during cytokinesis. It forms perpendicular to the axis of the spindle apparatus towards the end of telophase, in which sister chromatids are identically separated at the opposite sides of the spindle forming nuclei (Figure 1). The actomyosin ... | Actomyosin ring |
c_nexpqgozsrgb | The actomyosin ring operates in contractile motion, although the mechanism on how or what triggers the constriction is still an evolving topic. Other cytoskeletal proteins are also involved in maintaining the stability of the ring and driving its constriction. Apart from cytokinesis, in which the ring constricts as the... | Actomyosin ring |
c_3smh9zzui9oq | During this process, actin filaments are degraded, preserving the thickness of the ring. After cytokinesis is complete, one of the two daughter cells inherits a remnant known as the midbody ring.Activation of the cell-cycle kinase (e.g. Rho-kinases) during telophase initiates constriction of the actomyosin ring by crea... | Actomyosin ring |
c_h9rhfhwbmre1 | In molecular biology, an amplicon is a piece of DNA or RNA that is the source and/or product of amplification or replication events. It can be formed artificially, using various methods including polymerase chain reactions (PCR) or ligase chain reactions (LCR), or naturally through gene duplication. In this context, am... | Amplicon sequencing |
c_quee0ir4jjv0 | As it refers to the product of an amplification reaction, amplicon is used interchangeably with common laboratory terms, such as "PCR product." Artificial amplification is used in research, forensics, and medicine for purposes that include detection and quantification of infectious agents, identification of human remai... | Amplicon sequencing |
c_bpfa46yvok5n | In molecular biology, an annexin A5 affinity assay is a test to quantify the number of cells undergoing apoptosis. The assay uses the protein annexin A5 to tag apoptotic and dead cells, and the numbers are then counted using either flow cytometry or a fluorescence microscope.The annexin a5 protein binds to apoptotic ce... | Annexin A5 affinity assay |
c_9pcvi6mzonrb | In molecular biology, an arginine finger is an amino acid residue of some enzymes. Arginine fingers are often found in the protein superfamily of AAA+ ATPases, GTPases, and dUTPases, where they assist in the catalysis of the gamma phosphate or gamma and beta phosphates from ATP or GTP, which creates a release of energy... | Arginine finger |
c_79qs67tgrl9l | In molecular biology, an autotransporter domain is a structural domain found in some bacterial outer membrane proteins. The domain is always located at the C-terminal end of the protein and forms a beta-barrel structure. The barrel is oriented in the membrane such that the N-terminal portion of the protein, termed the ... | Autotransporter family |
c_krrl2lwhkg4y | These proteins are typically virulence factors, associated with infection or virulence in pathogenic bacteria. The name autotransporter derives from an initial understanding that the protein was self-sufficient in transporting the passenger domain through the outermembrane. This view has since been challenged by Benz a... | Autotransporter family |
c_84en08o5slmy | The type V(a), or autotransporter, secretion pathway constitutes the largest number of secreted virulence factors of any one of the seven known types of secretion in Gram-negative bacteria. This secretion pathway is exemplified by the prototypical IgA1 Protease of Neisseria gonorrhoeae. The protein is directed to the i... | Autotransporter family |
c_88y9unt9kbt6 | Once in the periplasm, the autotransporter domain inserts into the outer membrane. The passenger domain is passed through the center of the autotransporter domain to be presented on the outside of the cell, however the mechanism by which this occurs remains unclear.The C-terminal translocator domain corresponds to an o... | Autotransporter family |
c_aznbawq49pk0 | In those proteins where the cleavage is auto-catalytic, the peptidase domains belong to MEROPS peptidase families S6 and S8. Passenger domains structurally characterized to date have been shown to be dominated by a protein fold known as a beta helix, typified by pertactin. The folding of this domain is thought to be in... | Autotransporter family |
c_ijobd6g2e4ls | In molecular biology, an exonic splicing enhancer (ESE) is a DNA sequence motif consisting of 6 bases within an exon that directs, or enhances, accurate splicing of heterogeneous nuclear RNA (hnRNA) or pre-mRNA into messenger RNA (mRNA). | Exonic splicing enhancers |
c_ysrd3f7b7uf6 | In molecular biology, an inducer is a molecule that regulates gene expression. An inducer functions in two ways; namely: By disabling repressors. The gene is expressed because an inducer binds to the repressor. The binding of the inducer to the repressor prevents the repressor from binding to the operator. | Inducer |
c_qos3y0do76qc | RNA polymerase can then begin to transcribe operon genes. By binding to activators. | Inducer |
c_sca4aicyd8ua | Activators generally bind poorly to activator DNA sequences unless an inducer is present. Activator binds to an inducer and the complex binds to the activation sequence and activates target gene. Removing the inducer stops transcription.Because a small inducer molecule is required, the increased expression of the targe... | Inducer |
c_xwy2b95fj6yk | In molecular biology, an interactome is the whole set of molecular interactions in a particular cell. The term specifically refers to physical interactions among molecules (such as those among proteins, also known as protein–protein interactions, PPIs; or between small molecules and proteins) but can also describe sets... | Interactome |
c_nk8sdqhrk8pk | In molecular biology, an intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure, typically in the absence of its macromolecular interaction partners, such as other proteins or RNA. IDPs range from fully unstructured to partially structured and include random coil, ... | Intrinsically disordered proteins |
c_mfebq1o4fkfg | In molecular biology, an oscillating gene is a gene that is expressed in a rhythmic pattern or in periodic cycles. Oscillating genes are usually circadian and can be identified by periodic changes in the state of an organism. Circadian rhythms, controlled by oscillating genes, have a period of approximately 24 hours. F... | Gene oscillations |
c_5wlxhuty57sh | Other periods are also possible, such as 29.5 days resulting from circalunar rhythms or 12.4 hours resulting from circatidal rhythms. Oscillating genes include both core clock component genes and output genes. A core clock component gene is a gene necessary for to the pacemaker. However, an output oscillating gene, suc... | Gene oscillations |
c_mtaunnkfsxgn | In molecular biology, and more importantly high-throughput DNA sequencing, a chimera is a single DNA sequence originating when multiple transcripts or DNA sequences get joined. Chimeras can be considered artifacts and be filtered out from the data during processing to prevent spurious inferences of biological variation... | Chimera (molecular biology) |
c_e3qijifkm9kr | In a different context, the deliberate creation of artificial chimeras can also be a useful tool in molecular biology. For example, in protein engineering, "chimeragenesis" (forming chimeras between proteins that are encoded by homologous cDNAs) is one of the "two major techniques used to manipulate cDNA sequences". Fo... | Chimera (molecular biology) |
c_59367wtin7o5 | In molecular biology, apical membrane antigen 1 is a novel antigen of Plasmodium falciparum which has been cloned. It contains a hydrophobic domain typical of an integral membrane protein. The antigen is designated apical membrane antigen 1 (AMA-1) by virtue of appearing to be located in the apical complex. AMA-1 appea... | Apical membrane antigen 1 |
c_p1s95z3r2fqm | The 66kDa merozoite surface antigen (PK66) of Plasmodium knowlesi, a simian malaria, possesses vaccine-related properties believed to originate from a receptor-like role in parasite invasion of erythrocytes. The sequence of PK66 is conserved throughout Plasmodium, and shows high similarity to P. falciparum AMA-1. Follo... | Apical membrane antigen 1 |
c_nwokftajz9ts | Prior to rupture, the protein is concentrated at the apical end, following which it distributes itself entirely across the surface of the free merozoite. Immunofluorescence studies suggest that, during invasion, PK66 is excluded from the erythrocyte at, and behind, the invasion interface. == References == | Apical membrane antigen 1 |
c_a4tj8jsz33ce | In molecular biology, apovitellenin-1 is a family of proteins found in birds. As part of the avian reproductive effort, large quantities of triglyceride-rich very-low-density lipoprotein (VLDL) particles are transported by receptor-mediated endocytosis into the female germ cells, apovitellenin-1 is a protein component ... | Apovitellenin-1 |
c_n6tl0z6z3kb5 | This is because the VLDL particles are protected from lipolysis by apovitellenin-1a, which acts as a potent dimeric lipoprotein lipase inhibitor. Apo-VLDL-II is produced in the liver and secreted into the blood stream when induced by estrogen production in female birds. == References == | Apovitellenin-1 |
c_aj227nu987cj | In molecular biology, autophagy related 3 (Atg3) is the E2 enzyme for the LC3 lipidation process. It is essential for autophagy. The super protein complex, the Atg16L complex, consists of multiple Atg12-Atg5 conjugates. | ATG3 |
c_ac1c1ulof66s | Atg16L has an E3-like role in the LC3 lipidation reaction. The activated intermediate, LC3-Atg3 (E2), is recruited to the site where the lipidation takes place.Atg3 catalyses the conjugation of Atg8 and phosphatidylethanolamine (PE). Atg3 has an alpha/beta-fold, and its core region is topologically similar to canonical... | ATG3 |
c_zo4tdheh8s0s | Atg3 has two regions inserted in the core region and another with a long alpha-helical structure that protrudes from the core region as far as 30 A. It interacts with atg8 through an intermediate thioester bond between Cys-288 and the C-terminal Gly of atg8. It also interacts with the C-terminal region of the E1-like a... | ATG3 |
c_gfwo8tttorr4 | Atg3 is a ubiquitin like modifier that is topologically similar to the canonical E2 enzyme. It catalyses the conjugation of Atg8 and phosphatidylethanolamine.Atg3 consists of three domains, an N-terminal domain, a catalytic domain and a C-terminal domain. The catalytic domain contains a cysteine residue within an HPC m... | ATG3 |
c_1yc1v0njj041 | The small C-terminal domain is likely to be a distinct binding region for the stability of the autophagosome complex. It carries a highly characteristic conserved FLKF sequence motif. == References == | ATG3 |
c_ad8806h6gkc8 | In molecular biology, autotransporter proteins are proteins secreted out the Gram-negative bacteria. These beta helixes require a domain which is called the intramolecular autochaperone domain. It shows similarities with other intramolecular chaperone sequences and has a folding-associated function. This increases the ... | Autochaperone |
c_0818anyaqkdb | The autochaperone domain is usually located between the HSF and the passenger domain. When the passenger domain is translocated, starting with its C terminus, the autochaperone domain is first out. This would result in the formation of a hairpin structure. | Autochaperone |
c_s1jsqqi17faq | In molecular biology, bacterial DNA binding proteins are a family of small, usually basic proteins of about 90 residues that bind DNA and are known as histone-like proteins. Since bacterial binding proteins have a diversity of functions, it has been difficult to develop a common function for all of them. They are commo... | Bacterial DNA binding protein |
c_j3lpel4sw7ss | Eukaryotic histones package DNA to help it to fit in the nucleus, and they are known to be the most conserved proteins in nature. Examples include the HU protein in Escherichia coli, a dimer of closely related alpha and beta chains and in other bacteria can be a dimer of identical chains. HU-type proteins have been fou... | Bacterial DNA binding protein |
c_31pc5gx7m8v2 | In molecular biology, bacteriophage scaffolding proteins are proteins involved in bacteriophage assembly. The assembly of a macromolecular structure proceeds via a specific pathway of ordered events and involves conformational changes in the proteins as they join the assembly. The assembly process is aided by scaffoldi... | Bacteriophage scaffolding proteins |
c_2w5frrl4jukn | 240 copies of protein D form the external scaffold, while 60 copies of protein B form the internal scaffold. The role of scaffolding protein D is in the production of viral single-stranded RNA. == References == | Bacteriophage scaffolding proteins |
c_zqzx6lymv2t7 | In molecular biology, barrier-to-autointegration factor (BAF) is a family of essential proteins that is highly conserved in metazoan evolution, and which may act as DNA-bridging proteins. BAF binds directly to double-stranded DNA, to transcription activators, and to inner nuclear membrane proteins, including lamin A fi... | Barrier-to-autointegration factor |
c_ksay1ucay6sa | In molecular biology, binding domain is a protein domain which binds to a specific atom or molecule, such as calcium or DNA. A protein domain is a part of a protein sequence and a tertiary structure that can change or evolve, function, and live by itself independent of the rest of the protein chain. Upon binding, prote... | Binding domain |
c_pdr41lethk89 | In molecular biology, biochips are engineered substrates ("miniaturized laboratories") that can host large numbers of simultaneous biochemical reactions. One of the goals of biochip technology is to efficiently screen large numbers of biological analytes, with potential applications ranging from disease diagnosis to de... | Biochip |
c_dfxveg5eo7uk | In molecular biology, biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. This process often consists of metabolic pathways. | Biological synthesis |
c_w2mqpg36rtc9 | Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anab... | Biological synthesis |
c_xr7fyzof2mgo | The prerequisite elements for biosynthesis include: precursor compounds, chemical energy (e.g. ATP), and catalytic enzymes which may need coenzymes (e.g. NADH, NADPH). These elements create monomers, the building blocks for macromolecules. Some important biological macromolecules include: proteins, which are composed o... | Biological synthesis |
c_ba60yoox0gvr | In molecular biology, calmodulin binding domain (CaMBD) is a protein domain found in small-conductance calcium-activated potassium channels (SK channels). These channels are independent of voltage and gated solely by intracellular Ca2+. They are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca... | Calmodulin binding domain |
c_u9v30472p7fy | Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other. == Reference... | Calmodulin binding domain |
c_63c6sgy9437d | In molecular biology, cia-dependent small RNAs (csRNAs) are small RNAs produced by Streptococci. These RNAs are part of the regulon of the CiaRH two-component regulatory system. Two of these RNAs, csRNA4 and csRNA5, have been shown to affect stationary-phase autolysis. | Cia-dependent small RNAs |
c_fdbag7lux4ml | In molecular biology, cob(I)yrinic acid a,c-diamide adenosyltransferase (also known as ATP:cob(I)alamin adenosyltransferase or ATP:corrinoid adenosyltransferase) EC 2.5.1.17 is an enzyme which catalyses the conversion of cobalamin (vitamin B12) into one of its coenzyme forms, adenosylcobalamin (coenzyme B12, AdoCbl). A... | Cob(I)yrinic acid a,c-diamide adenosyltransferase |
c_7imi92pbf3r7 | Each of the three enzyme types appears to be specialised for particular AdoCbl-dependent enzymes or for the de novo synthesis of AdoCbl. PduO and EutT are distantly related, sharing short conserved motifs, while CobA is evolutionarily unrelated and is an example of convergent evolution. The CobA group includes the ATP:... | Cob(I)yrinic acid a,c-diamide adenosyltransferase |
c_hiowhkog6l40 | There is a high degree of sequence identity between these proteins. CobA is responsible for attaching the adenosyl moiety from ATP to the cobalt ion of the corrin ring, necessary for the conversion of cobalamin to adenosylcobalamin. PduO functions to convert cobalamin to AdoCbl for 1,2-propanediol degradation, while Eu... | Cob(I)yrinic acid a,c-diamide adenosyltransferase |
c_ar1ftuai4ezg | In molecular biology, communication between neurons typically occurs by chemical transmission across gaps between the cells called synapses. The transmitted chemicals, known as neurotransmitters, regulate a significant fraction of vital body functions. It is possible to anatomically locate neurotransmitters by labeling... | Molecular Neuroscience |
c_g3il41db2u5m | This can give rise to formaldehyde-induced fluorescence when exposed to ultraviolet light. Dopamine, a catecholamine, was identified in the nematode C. elegans by using this technique.Immunocytochemistry, which involves raising antibodies against targeted chemical or biological entities, includes a few other techniques... | Molecular Neuroscience |
c_9n4yyqxbw4p5 | In molecular biology, complementarity describes a relationship between two structures each following the lock-and-key principle. In nature complementarity is the base principle of DNA replication and transcription as it is a property shared between two DNA or RNA sequences, such that when they are aligned antiparallel ... | Complementary base sequence |
c_9zcr6iae1nvu | Furthermore, various DNA repair functions as well as regulatory functions are based on base pair complementarity. In biotechnology, the principle of base pair complementarity allows the generation of DNA hybrids between RNA and DNA, and opens the door to modern tools such as cDNA libraries. While most complementarity i... | Complementary base sequence |
c_1rd1nlovy6fv | In molecular biology, copines is a name for the group of human proteins that includes members such as CPNE1, CPNE4, CPNE6, and CPNE8. These are highly conserved, calcium-dependent membrane proteins found in a variety of eukaryotes. The domain structure of these 55 kDa proteins suggests that they may have a role in memb... | Copine |
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