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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 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'' (bacter ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
010 Large Subunit-1FFK
1 (one, unit, unity) is a number representing a single or the only entity. 1 is also a numerical digit and represents a single unit of counting or measurement. For example, a line segment of ''unit length'' is a line segment of length 1. In conventions of sign where zero is considered neither positive nor negative, 1 is the first and smallest positive integer. It is also sometimes considered the first of the infinite sequence of natural numbers, followed by 2, although by other definitions 1 is the second natural number, following 0. The fundamental mathematical property of 1 is to be a multiplicative identity, meaning that any number multiplied by 1 equals the same number. Most if not all properties of 1 can be deduced from this. In advanced mathematics, a multiplicative identity is often denoted 1, even if it is not a number. 1 is by convention not considered a prime number; this was not universally accepted until the mid-20th century. Additionally, 1 is the s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
X-ray Crystallography
X-ray crystallography is the experimental science determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract into many specific directions. By measuring the angles and intensities of these diffracted beams, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal. From this electron density, the mean positions of the atoms in the crystal can be determined, as well as their chemical bonds, their crystallographic disorder, and various other information. Since many materials can form crystals—such as salts, metals, minerals, semiconductors, as well as various inorganic, organic, and biological molecules—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 among various mat ... [...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 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.Branden C. and Tooze J. "Introduction to Protein Structure" Garland Publishing, New York. 1990 and 1991. A number of tertiary structures may fold into a quaternary structure.Kyte, J. "Structure in Protein Chemistry." Garland Publishing, New York. 1995. 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 polypept ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptidyl Transferase
The peptidyl transferase is an aminoacyltransferase () as well as the primary enzymatic function of the ribosome, which forms peptide bonds between adjacent amino acids using tRNAs during the translation process of protein biosynthesis. The substrates for the peptidyl transferase reaction are two tRNA molecules, one bearing the growing peptide chain and the other bearing the amino acid that will be added to the chain. The peptidyl chain and the amino acids are attached to their respective tRNAs via ester bonds to the O atom at the CCA-3' ends of these tRNAs. Peptidyl transferase is an enzyme that catalyzes the addition of an amino acid residue in order to grow the polypeptide chain in protein synthesis. It is located in the large ribosomal subunit, where it catalyzes the peptide bond formation. It is composed entirely of RNA. The alignment between the CCA ends of the ribosome-bound peptidyl tRNA and aminoacyl tRNA in the peptidyl transferase center contribute to its ability to cat ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Secondary Structure
Protein secondary structure is the three dimensional conformational isomerism, form of ''local segments'' of proteins. 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 residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 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 peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ... [...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 small and 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 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 by mass. Structure Although the primary structure of rRNA sequences can vary across organisms, base-pairing within these sequences commonly forms stem-loop configurations. The length and position of these rRNA stem-loops allow them to create three-di ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nucleotide
Nucleotides are organic molecules consisting of a nucleoside 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-forms on Earth. Nucleotides are obtained in the diet and are also synthesized from common nutrients by the liver. Nucleotides are composed of three subunit molecules: a nucleobase, a 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 triphosphate (UTP)—throughout the cell for the many cellular func ... [...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, a prestigious college preparatory school 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 ... [...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 synthetases ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Deinococcus Radiodurans
''Deinococcus radiodurans'' is an extremophilic bacterium and one of the most radiation-resistant organisms known. It can survive cold, dehydration, vacuum, and acid, and therefore is known as a polyextremophile. It has been listed as the world's toughest known bacterium in ''The Guinness Book Of World Records''. 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 Bacterium”, in reference to Conan the Barbarian. Initially, it was placed in the genus ''Micrococcus''. After evaluation of ribosomal RNA sequences and other evidence, it was placed in its own genus ''Deinococcus'', which is closely related to the genus ''Thermus''. ''Deinococcus'' is one genus of three in the order ''Deinococcale ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
