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Ribonuclease T1
Ribonuclease T1 (, ''guanyloribonuclease'', ''Aspergillus oryzae ribonuclease'', ''RNase N1'', ''RNase N2'', ''ribonuclease N3'', ''ribonuclease U1'', ''ribonuclease F1'', ''ribonuclease Ch'', ''ribonuclease PP1'', ''ribonuclease SA'', ''RNase F1'', ''ribonuclease C2'', ''binase'', ''RNase Sa'', ''guanyl-specific RNase'', ''RNase G'', ''RNase T1'', ''ribonuclease guaninenucleotido-2'-transferase (cyclizing)'', ''ribonuclease N3'', ''ribonuclease N1'') is a fungal endonuclease that cleaves single-stranded RNA after guanine residues, i.e., on their 3' end; the most commonly studied form of this enzyme is the version found in the mold ''Aspergillus oryzae''. Owing to its specificity for guanine, RNase T1 is often used to digest denatured RNA prior to sequencing. Similar to other ribonucleases such as barnase and RNase A, ribonuclease T1 has been popular for folding studies. Structurally, ribonuclease T1 is a small α+β protein (104 amino acids) with a four-stranded, antiparallel ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aspergillus Oryzae
''Aspergillus oryzae'', also known as , is a filamentous fungus (a mold) used in East Asia to saccharify rice, sweet potato, and barley in the making of alcoholic beverages such as ''sake'' and '' shōchū'', and also to ferment soybeans for making soy sauce and ''miso''. However, in the production of fermented foods of soybeans such as soy sauce and ''miso'', '' Aspergillus sojae'' is sometimes used instead of ''A. oryzae''. Incidentally, in China and Korea, the fungi used for fermented foods for a long time in the production of traditional alcoholic beverages were not ''A. oryzae'' but fungi belonging to ''Rhizopus'' and ''Mucor''. '' A. oryzae'' is also used for the production of rice vinegars. Barley ''kōji'' (麦麹) or rice ''kōji'' (米麹) are made by fermenting the grains with ''A. oryzae'' hyphae. Genomic analysis has led some scholars to believe that the Japanese domesticated the ''Aspergillus flavus'' that had mutated and ceased to produce toxic aflatoxins, givi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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, notably Alzheimer's disease. 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 refined versi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Biochemistry (journal)
''Biochemistry'' is a peer-reviewed academic journal in the field of biochemistry. Founded in 1962, the journal is now published weekly by the American Chemical Society, with 51 or 52 annual issues. The journal's 2015 impact factor was 2.876, and it received a total of 79,348 citations in 2015.''Biochemistry'': About (accessed May 24, 2017) The previous editor-in-chief was Richard N. Armstrong () (2004–16). After his death, ( |
Peptide Bond
In organic chemistry, a peptide bond is an amide type of covalent chemical bond linking two consecutive alpha-amino acids from C1 (carbon number one) of one alpha-amino acid and N2 (nitrogen number two) of another, along a peptide or protein chain. It can also be called a eupeptide bond to distinguish it from an isopeptide bond, which is another type of amide bond between two amino acids. Synthesis When two amino acids form a ''dipeptide'' through a ''peptide bond'', it is a type of condensation reaction. In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other. One loses a hydrogen and oxygen from its carboxyl group (COOH) and the other loses a hydrogen from its amino group (NH2). This reaction produces a molecule of water (H2O) and two amino acids joined by a peptide bond (−CO−NH−). The two joined amino acids are called a dipeptide. The am ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Isomer
In chemistry, isomers are molecules or polyatomic ions with identical molecular formulae – that is, same number of atoms of each element – but distinct arrangements of atoms in space. Isomerism is existence or possibility of isomers. Isomers do not necessarily share similar chemical or physical properties. Two main forms of isomerism are structural or constitutional isomerism, in which ''bonds'' between the atoms differ; and stereoisomerism or spatial isomerism, in which the bonds are the same but the ''relative positions'' of the atoms differ. Isomeric relationships form a hierarchy. Two chemicals might be the same constitutional isomer, but upon deeper analysis be stereoisomers of each other. Two molecules that are the same stereoisomer as each other might be in different conformational forms or be different isotopologues. The depth of analysis depends on the field of study or the chemical and physical properties of interest. The English word "isomer" () is a back-for ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proline
Proline (symbol Pro or P) is an organic acid classed as a proteinogenic amino acid (used in the biosynthesis of proteins), although it does not contain the amino group but is rather a secondary amine. The secondary amine nitrogen is in the protonated form (NH2+) under biological conditions, while the carboxyl group is in the deprotonated −COO− form. The "side chain" from the α carbon connects to the nitrogen forming a pyrrolidine loop, classifying it as a aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it from the non-essential amino acid L-glutamate. It is encoded by all the codons starting with CC (CCU, CCC, CCA, and CCG). Proline is the only proteinogenic secondary amino acid which is a secondary amine, as the nitrogen atom is attached both to the α-carbon and to a chain of three carbons that together form a five-membered ring. History and etymology Proline was first isolated in 1900 by Richard Willstätter who obtained the amino ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Journal Of Biochemistry
''The Journal of Biochemistry'' is a peer-reviewed scientific journal that covers research on biochemistry, molecular biology, cell biology, and biotechnology. It was established in 1922 and is published by Oxford University Press on behalf of the Japanese Biochemical Society. The editor-in-chief is Kohei Miyazono (Tokyo University). According to the ''Journal Citation Reports'', the journal has a 2020 impact factor of 3.387. Article types ''The Journal of Biochemistry'' publishes Regular Papers (original scientific work), Rapid Communications (complete, yet brief, accounts of work), and Reviews (short reviews solicited by the editorial board The editorial board is a group of experts, usually at a publication, who dictate the tone and direction the publication's editorial policy will take. Mass media At a newspaper, the editorial board usually consists of the editorial page editor, a ...). References External links * {{Official website, http://jb.oxfordjournals.org/ Japane ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Journal Of Biological Chemistry
The ''Journal of Biological Chemistry'' (''JBC'') is a weekly peer-reviewed scientific journal that was established in 1905., jbc.org Since 1925, it is published by the American Society for Biochemistry and Molecular Biology. It covers research in areas of biochemistry and molecular biology. The editor is Alex Toker. As of January 2021, the journal is fully open access. In press articles are available free on its website immediately after acceptance. Editors The following individuals have served as editors of the journal: * 1906–1909: John Jacob Abel and Christian Archibald Herter * 1909–1910: Christian Archibald Herter * 1910–1914: Alfred Newton Richards * 1914–1925: Donald D. Van Slyke * 1925–1936: Stanley R. Benedict. After Benedict died, John T. Edsall served as temporary editor until the next editor was appointed. * 1937–1958: Rudolph J. Anderson * 1958–1967: John T. Edsall * 1968–1971: William Howard Stein * 1971–2011: Herbert Tabor * 2011–2015: ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha Helix
The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a right hand-helix conformation in which every backbone N−H group hydrogen bonds to the backbone C=O group of the amino acid located four residues earlier along the protein sequence. The alpha helix is also called a classic Pauling–Corey–Branson α-helix. The name 3.613-helix is also used for this type of helix, denoting the average number of residues per helical turn, with 13 atoms being involved in the ring formed by the hydrogen bond. Among types of local structure in proteins, the α-helix is the most extreme and the most predictable from sequence, as well as the most prevalent. Discovery In the early 1930s, William Astbury showed that there were drastic changes in the X-ray fiber diffraction of moist wool or hair fibers upon significant stretching. The data suggested that the unstretched fibers had a coiled molecular structure with a characteristic repeat of ≈. Astb ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Amino Acid
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although hundreds of amino acids exist in nature, by far the most important are the alpha-amino acids, which comprise proteins. Only 22 alpha amino acids appear in the genetic code. Amino acids can be classified according to the locations of the core structural functional groups, as Alpha and beta carbon, alpha- , beta- , gamma- or delta- amino acids; other categories relate to Chemical polarity, polarity, ionization, and side chain group type (aliphatic, Open-chain compound, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acid '' residues'' form the second-largest component (water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling life ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Journal Of Molecular Biology
The ''Journal of Molecular Biology'' is a biweekly peer-reviewed scientific journal covering all aspects of molecular biology. It was established in 1959 and is published by Elsevier. The editor-in-chief is Peter Wright ( The Scripps Research Institute). Abstracting and indexing The journal is abstracted and indexed in: According to the ''Journal Citation Reports'', the journal has a 2020 impact factor of 5.469. Notable articles Some of the most highly cited articles that have appeared in the journal are: *, in which Jacques Monod, Jeffries Wyman, and Jean-Pierre Changeux presented the MWC model, that explained the cooperativity exhibited by allosteric proteins, such as hemoglobin. *, in which Edwin Southern presented the first description of nucleic acid blotting, a technique that revolutionized the field of molecular biology. *, in which the Smith–Waterman algorithm for determining the degree of homology of DNA, RNA, or protein sequences was first described. *, in which ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Angewandte Chemie
''Angewandte Chemie'' (, meaning "Applied Chemistry") is a weekly peer-reviewed scientific journal that is published by Wiley-VCH on behalf of the German Chemical Society (Gesellschaft Deutscher Chemiker). Publishing formats include feature-length reviews, short highlights, research communications, minireviews, essays, book reviews, meeting reviews, correspondences, corrections, and obituaries. This journal contains review articles covering all aspects of chemistry. According to the ''Journal Citation Reports'', the journal had a 2021 impact factor of 16.823. Editions The journal appears in two editions with separate volume and page numbering: a German edition, ''Angewandte Chemie'' ( (print), (online)), and a fully English-language edition, ''Angewandte Chemie International Edition'' ( (print), (online)). The editions are identical in content with the exception of occasional reviews of German-language books or German translations of IUPAC recommendations. Business model ''A ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
