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Bacteriophage MS2
Bacteriophage MS2 (''Emesvirus zinderi''), commonly called MS2, is an icosahedral, positive-sense single-stranded RNA virus that infects the bacterium ''Escherichia coli'' and other members of the Enterobacteriaceae. MS2 is a member of a family of closely related bacterial viruses that includes bacteriophage f2, bacteriophage Qβ, R17, and GA. It is small and contains a maturation protein, coat protein, and genomic RNA. It also has one of the smallest known genomes, encoding four proteins. The MS2 lifecycle involves infecting bacteria with the fertility factor, enabling the virus to attach to the pilus, though the mechanism by which the virus's RNA enters the bacterium remains unknown. Once inside, the viral RNA starts functioning as a messenger RNA to produce viral proteins. MS2 replicates its plus-strand genome by creating a minus strand RNA as a template. The virus then assembles, and the bacterial cell lyses, releasing new viruses. The virus was isolated in 1961 and it ...
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Viral Capsid
A capsid is the protein shell of a virus, enclosing its genetic material. It consists of several oligomeric (repeating) structural subunits made of protein called protomers. The observable 3-dimensional morphological subunits, which may or may not correspond to individual proteins, are called capsomeres. The proteins making up the capsid are called capsid proteins or viral coat proteins (VCP). The virus genomic component inside the capsid, along with occasionally present virus core protein, is called the virus core. The capsid and core together are referred to as a nucleocapsid (cf. also virion). Capsids are broadly classified according to their structure. The majority of the viruses have capsids with either helical or icosahedral structure. Some viruses, such as bacteriophages, have developed more complicated structures due to constraints of elasticity and electrostatics. The icosahedral shape, which has 20 equilateral triangular faces, approximates a sphere, while the h ...
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Virion
A virion (plural, ''viria'' or ''virions'') is an inert virus particle capable of invading a Cell (biology), cell. Upon entering the cell, the virion disassembles and the genetic material from the virus takes control of the cell infrastructure, thus enabling the virus to Replication (virus), replicate. The genetic material (''Viral core, core'', either DNA or RNA, along with occasionally present virus core protein) inside the virion is usually enclosed in a protection shell, known as the capsid. While the terms "virus" and "virion" are occasionally confused, recently "virion" is used solely to describe the virus structure outside of cells, while the terms "virus/viral" are broader and also include biological properties such as the infectivity of a virion. Components A virion consists of one or more nucleic acid genome molecules (single-stranded or double-stranded RNA or DNA) and coatings (a capsid and possibly a viral envelope). The virion may contain other proteins (for examp ...
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Stem-loop
Stem-loops are nucleic acid Biomolecular structure, secondary structural elements which form via intramolecular base pairing in single-stranded DNA or RNA. They are also referred to as hairpins or hairpin loops. A stem-loop occurs when two regions of the same nucleic acid strand, usually Complementarity (molecular biology), complementary in nucleotide sequence, base-pair to form a double helix that ends in a loop of unpaired nucleotides. Stem-loops are most commonly found in RNA, and are a key building block of many RNA biomolecular structure#Secondary structure, secondary structures. Stem-loops can direct RNA folding, protect structural stability for messenger RNA (mRNA), provide recognition sites for RNA-binding protein, RNA binding proteins, and serve as a Substrate (chemistry), substrate for Enzyme catalysis, enzymatic reactions. Formation and stability The formation of a stem-loop is dependent on the stability of the helix and loop regions. The first prerequisite is the p ...
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Ribosome
Ribosomes () are molecular machine, macromolecular machines, found within all cell (biology), cells, that perform Translation (biology), biological protein synthesis (messenger RNA translation). Ribosomes link amino acids together in the order specified by the codons of messenger RNA molecules to form polypeptide chains. Ribosomes consist of two major components: the small and large ribosomal subunits. Each subunit consists of one or more ribosomal RNA molecules and many ribosomal proteins (). The ribosomes and associated molecules are also known as the ''translational apparatus''. Overview The sequence of DNA that encodes the sequence of the amino acids in a protein is transcribed into a messenger RNA (mRNA) chain. Ribosomes bind to the messenger RNA molecules and use the RNA's sequence of nucleotides to determine the sequence of amino acids needed to generate a protein. Amino acids are selected and carried to the ribosome by transfer RNA (tRNA) molecules, which enter the riboso ...
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Bacterial Conjugation
Bacterial conjugation is the transfer of genetic material between Bacteria, bacterial cells by direct cell-to-cell contact or by a bridge-like connection between two cells. This takes place through a pilus. It is a parasexual cycle, parasexual mode of reproduction in bacteria. It is a mechanism of horizontal gene transfer as are Transformation (genetics), transformation and Transduction (genetics), transduction although these two other mechanisms do not involve cell-to-cell contact. Classical ''E. coli'' bacterial conjugation is often regarded as the bacterial equivalent of sexual reproduction or mating, since it involves the exchange of genetic material. However, it is not sexual reproduction, since no exchange of gamete occurs, and indeed no biogenesis, generation of a new organism: instead, an existing organism is transformed. During classical ''E. coli'' conjugation, the ''donor'' cell provides a conjugative or mobilizable genetic element that is most often a plasmid or trans ...
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Plasmid
A plasmid is a small, extrachromosomal DNA molecule within a cell that is physically separated from chromosomal DNA and can replicate independently. They are most commonly found as small circular, double-stranded DNA molecules in bacteria and archaea; however plasmids are sometimes present in and eukaryotic organisms as well. Plasmids often carry useful genes, such as those involved in antibiotic resistance, virulence, secondary metabolism and bioremediation. While chromosomes are large and contain all the essential genetic information for living under normal conditions, plasmids are usually very small and contain additional genes for special circumstances. Artificial plasmids are widely used as vectors in molecular cloning, serving to drive the replication of recombinant DNA sequences within host organisms. In the laboratory, plasmids may be introduced into a cell via transformation. Synthetic plasmids are available for procurement over the internet by various vendors ...
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Fertility Factor (bacteria)
The F-plasmid (first named F by one of its discoverers Esther Lederberg;also called the sex factor in ''E. coli'',the F sex factor, the fertility factor, or simply the F factor) allows genes to be transferred from one bacterium carrying the factor to another bacterium lacking the factor by conjugation. The F factor was the first plasmid to be discovered. Unlike other plasmids, F factor is constitutive for transfer proteins due to a mutation in the gene ''finO''. The F plasmid belongs to F-like plasmids, a class of conjugative plasmids that control sexual functions of bacteria with a fertility inhibition (Fin) system. Discovery Esther M. Lederberg and Luigi L. Cavalli-Sforza discovered "F," subsequently publishing with Joshua Lederberg. Once her results were announced, two other labs joined the studies. "This was not a simultaneous independent discovery of F (I named this as Fertility Factor until it was understood.) We wrote to Hayes, Jacob, & Wollman who then proceeded ...
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Beta Hairpin
The beta hairpin (sometimes also called beta-ribbon or beta-beta unit) is a simple protein structural motif involving two beta strands that look like a Hairpin (fashion), hairpin. The motif consists of two strands that are adjacent in primary structure, oriented in an Antiparallel (biochemistry), antiparallel direction (the N-terminus of one sheet is adjacent to the C-terminus of the next), and linked by a short loop of two to five amino acids. Beta hairpins can occur in isolation or as part of a series of hydrogen bonded strands that collectively comprise a beta sheet. Researchers such as Francisco J. Blanco, Francisco Blanco ''et al.'' have used protein NMR to show that beta-hairpins can be formed from isolated short peptides in aqueous solution, suggesting that hairpins could form nucleation sites for protein folding. Classification Beta hairpins were originally categorized solely by the number of amino acid residues in their loop sequences, such that they were named one-resid ...
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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 ...
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Beta Sheet
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. ...
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Applied And Environmental Microbiology
''Applied and Environmental Microbiology'' is a biweekly peer-reviewed scientific journal published by the American Society for Microbiology. It was established in 1953 as ''Applied Microbiology'' and obtained its current name in 1975. Articles older than six months are available free of cost from the website, however, the newly published articles within six months are available to subscribers only. According to the ''Journal Citation Reports'', the journal has a 2023 impact factor of 3.9. The journal has been ranked as one of the top 100 journals over the past 100 years in the fields of biology and medicine. Special Libraries Association100 Journals in last 100 years/ref> The editor-in-chief is Gemma Reguera (Michigan State University Michigan State University (Michigan State or MSU) is a public university, public Land-grant university, land-grant research university in East Lansing, Michigan, United States. It was founded in 1855 as the Agricultural College of the State o ...
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Isoelectric Point
The isoelectric point (pI, pH(I), IEP), is the pH at which a molecule carries no net electric charge, electrical charge or is electrically neutral in the statistical mean. The standard nomenclature to represent the isoelectric point is pH(I). However, pI is also used. For concision, brevity, this article uses pI. The net charge on the molecule is affected by pH of its surrounding environment and can become more positively or negatively charged due to the gain or loss, respectively, of protons#In Physics and biochemistry, protons (H+). Surfaces naturally charge to form a double layer (interfacial), double layer. In the common case when the surface charge-determining ions are H+/HO−, the net surface charge is affected by the pH of the liquid in which the solid is submerged. The pI value can affect the solubility of a molecule at a given pH. Such molecules have minimum solubility in water or salt solutions at the pH that corresponds to their pI and often precipitate out of Solutio ...
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