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Prokaryotic Large Ribosomal Subunit
50 S is the larger subunit of the 70S ribosome of prokaryotes, i.e. bacteria and archaea. It is the site of inhibition for antibiotics such as macrolides, chloramphenicol, clindamycin, and the pleuromutilins. It includes the 5S ribosomal RNA and 23S ribosomal RNA. Despite having the same sedimentation rate, bacterial and archaeal ribosomes can be quite different. Structure 50S, roughly equivalent to the 60S ribosomal subunit in eukaryotic cells, is the larger subunit of the 70S ribosome of prokaryotes. The 50S subunit is primarily composed of proteins but also contains single-stranded RNA known as ribosomal RNA (rRNA). rRNA forms secondary and tertiary structures to maintain the structure and carry out the catalytic functions of the ribosome. X-ray crystallography has yielded electron density maps allowing the structure of the 50S in ''Haloarcula marismortui'' (archaeon) to be determined to 2.4 Å resolutionand of the 50S in the ''Deinococcus radiodurans'' (bacterium) to 3 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
010 Large Subunit-1FFK
1 (one, unit, unity) is a number, numeral, and glyph. It is the first and smallest positive integer of the infinite sequence of natural numbers. This fundamental property has led to its unique uses in other fields, ranging from science to sports, where it commonly denotes the first, leading, or top thing in a group. 1 is the unit of counting or measurement, a determiner for singular nouns, and a gender-neutral pronoun. Historically, the representation of 1 evolved from ancient Sumerian and Babylonian symbols to the modern Arabic numeral. In mathematics, 1 is the multiplicative identity, meaning that any number multiplied by 1 equals the same number. 1 is by convention not considered a prime number. In digital technology, 1 represents the "on" state in binary code, the foundation of computing. Philosophically, 1 symbolizes the ultimate reality or source of existence in various traditions. In mathematics The number 1 is the first natural number after 0. Each natural number, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
X-ray Crystallography
X-ray crystallography is the experimental science of determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to Diffraction, diffract in specific directions. By measuring the angles and intensities of the X-ray diffraction, a crystallography, crystallographer can produce a three-dimensional picture of the density of electrons within the crystal and the positions of the atoms, as well as their chemical bonds, crystallographic disorder, and other information. X-ray crystallography has been fundamental in the development of many scientific fields. In its first decades of use, this method determined the size of atoms, the lengths and types of chemical bonds, and the atomic-scale differences between various materials, especially minerals and alloys. The method has also revealed the structure and function of many biological molecules, including vitamins, drugs, proteins and nucleic acids such as DNA. X-ray crystall ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tertiary Structure
Protein tertiary structure is the three-dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains and the backbone may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure. A number of these structures may bind to each other, forming a quaternary structure. History The science of the tertiary structure of proteins has progressed from one of hypothesis to one of detailed definition. Although Emil Fischer had suggested proteins were made of polypeptide chains and amino acid side chains, it was Dorothy Maud Wrinch who incorporated geometry into the prediction of protein structures. Wrinch demon ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptidyl Transferase
The peptidyl transferase center (, PTC) is an Aminoacyltransferases, aminoacyltransferase ribozyme (RNA enzyme) located in the large subunit of the ribosome. It forms peptide bonds between adjacent amino acids during the Translation (genetics), translation process of protein biosynthesis. It is also responsible for peptidyl-tRNA hydrolysis, allowing the release of the synthesized peptide chain at the end of translation. Peptidyl transferase activity is not mediated by any ribosomal proteins, but entirely by ribosomal RNA (rRNA). The catalytic activity of the PTC is a significant piece of evidence supporting the RNA World hypothesis. The PTC is a highly conserved region with a very slow rate of mutation. It is considered to be among the most ancient elements of the ribosome, probably predating the last universal common ancestor. The position of the PTC is analogous in all ribosomes (domain V in 23S numbering), being a part of the large subunit ribosomal RNA with the name only va ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Secondary Structure
Protein secondary structure is the local spatial conformation of the polypeptide backbone excluding the side chains. The two most common Protein structure#Secondary structure, secondary structural elements are alpha helix, alpha helices and beta sheets, though beta turns and omega loops occur as well. Secondary structure elements typically spontaneously form as an intermediate before the protein protein folding, folds into its three dimensional protein tertiary structure, tertiary structure. Secondary structure is formally defined by the pattern of hydrogen bonds between the Amine, amino hydrogen and carboxyl oxygen atoms in the peptide backbone chain, backbone. Secondary structure may alternatively be defined based on the regular pattern of backbone Dihedral angle#Dihedral angles of proteins, dihedral angles in a particular region of the Ramachandran plot regardless of whether it has the correct hydrogen bonds. The concept of secondary structure was first introduced by Kaj Ulrik ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residue (biochemistry), residues. Proteins perform a vast array of functions within organisms, including Enzyme catalysis, catalysing metabolic reactions, DNA replication, Cell signaling, responding to stimuli, providing Cytoskeleton, structure to cells and Fibrous protein, organisms, and Intracellular transport, transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the Nucleic acid sequence, nucleotide sequence of their genes, and which usually results in protein folding into a specific Protein structure, 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called pep ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
RRNA
Ribosomal ribonucleic acid (rRNA) is a type of non-coding RNA which is the primary component of ribosomes, essential to all cells. rRNA is a ribozyme which carries out protein synthesis in ribosomes. Ribosomal RNA is transcribed from ribosomal DNA (rDNA) and then bound to ribosomal proteins to form SSU rRNA, small and LSU rRNA, large ribosome subunits. rRNA is the physical and mechanical factor of the ribosome that forces transfer RNA (tRNA) and messenger RNA (mRNA) to process and Translation (biology), translate the latter into proteins. Ribosomal RNA is the predominant form of RNA found in most cells; it makes up about 80% of cellular RNA despite never being translated into proteins itself. Ribosomes are composed of approximately 60% rRNA and 40% ribosomal proteins, though this ratio differs between Prokaryote, prokaryotes and Eukaryote, eukaryotes. Structure Although the primary structure of rRNA sequences can vary across organisms, Base pair, base-pairing within these sequ ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nucleotide
Nucleotides are Organic compound, organic molecules composed of a nitrogenous base, a pentose sugar and a phosphate. They serve as monomeric units of the nucleic acid polymers – deoxyribonucleic acid (DNA) and ribonucleic acid (RNA), both of which are essential biomolecules within all Life, life-forms on Earth. Nucleotides are obtained in the diet and are also synthesized from common Nutrient, nutrients by the liver. Nucleotides are composed of three subunit molecules: a nucleobase, a pentose, five-carbon sugar (ribose or deoxyribose), and a phosphate group consisting of one to three phosphates. The four nucleobases in DNA are guanine, adenine, cytosine, and thymine; in RNA, uracil is used in place of thymine. Nucleotides also play a central role in metabolism at a fundamental, cellular level. They provide chemical energy—in the form of the nucleoside triphosphates, adenosine triphosphate (ATP), guanosine triphosphate (GTP), cytidine triphosphate (CTP), and uridine triph ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peter Moore (chemist)
Peter B. Moore (born October 15, 1939) is Sterling Professor emeritus of Chemistry, Professor of Molecular Biophysics and Biochemistry at Yale University. He has dedicated his entire career to understanding the structure, function, and mechanism of the ribosome. Moore was born in Boston, Massachusetts, in 1939 to Laura Bartlett Moore and Francis Daniels Moore. He received his B.S. degree in biophysics from Yale University in 1961, and his Ph.D. in biophysics from Harvard University in 1966, where he worked in the laboratory of James D. Watson. Prior to attending Yale, Moore graduated from Milton Academy in Milton, Massachusetts, where he was elected to the Cum Laude Society. As a postdoctoral fellow and a sabbatical visitor, he has done research at the University of Geneva, Switzerland (with A. Tissieres), at the Medical Research Council Laboratory of Molecular Biology, Cambridge, England (with Hugh E. Huxley), and at the University of Oxford, England. He is a fellow of the A ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thomas Steitz
Thomas Arthur Steitz (August 23, 1940 – October 9, 2018) was an American biochemist, a Sterling Professor of Molecular Biophysics and Biochemistry at Yale University, and investigator at the Howard Hughes Medical Institute, best known for his pioneering work on the ribosome. Steitz was awarded the 2009 Nobel Prize in Chemistry along with Venkatraman Ramakrishnan and Ada Yonath "for studies of the structure and function of the ribosome".2009 Nobel Prize in Chemistry Nobel Foundation. Steitz also won the Gairdner International Award in 2007Thomas Steitz Thomas Steitz Lab. "for his studies on the structure and function of the [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nenad Ban
Nenad Ban is a biochemist born in Zagreb, Croatia who currently works at the ETH Zurich, Swiss Federal Institute of Technology, as a professor of Structural Molecular Biology. He is a pioneer in studying gene expression mechanisms and the participating protein synthesis machinery. Career Nenad Ban was born in 1966 in Zagreb. His parents, Jasna and Zvonimir, were scientists and university professors. He received a degree in molecular biology at the Faculty of Science, University of Zagreb and decided to continue with his studies in the United States where he obtained a PhD degree at the University of California, Riverside in the laboratory of Alexander McPherson. He carried out his postdoctoral studies at Yale University in the laboratory of Thomas A. Steitz. Already in high school he developed an interest in understanding the mechanisms of protein synthesis, which led him to the laboratory of Prof. Zeljko Kucan and Ivana Weygand in Zagreb where he investigated tRNA synthetase ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Deinococcus Radiodurans
''Deinococcus radiodurans'' is a bacterium, an extremophile and one of the most radiation-resistant organisms known. It can survive cold, dehydration, vacuum, and acid, and therefore is known as a polyextremophile. ''The Guinness Book Of World Records'' listed it in January 1998 as the world's most radiation-resistant bacterium or lifeform. Several bacteria of comparable radioresistance are known, including some species of the genus '' Chroococcidiopsis'' (phylum cyanobacteria) and some species of '' Rubrobacter'' (phylum Actinomycetota); among the archaea, the species '' Thermococcus gammatolerans'' shows comparable radioresistance. Name and classification The name ''Deinococcus radiodurans'' derives from the Ancient Greek δεινός () and κόκκος () meaning "terrible grain/berry" and the Latin and , meaning "radiation-surviving". The species was formerly called ''Micrococcus radiodurans''. As a consequence of its hardiness, it has been nicknamed “Conan the Bacteri ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
