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II. Beta oxidation of fatty acid
II. Beta oxidation of fatty acid

... A. RNA polymerase II has 3’-5’ exonuclease activity and can proofread its work B. DNA polymerase II has 3’-5’ exonuclease activity and can proofread its work C. mRNA half-life is short and mRNA is not passed on to the cell’s progeny D. Ribosomes can bypass errors in mRNA transcript and continue with ...
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... 3 different species: 5S, 23S and 16S; incorporated into either the 50S or 30S ribosomal subunits. Play important structural, functional, and catalytic roles in the ribosome ...
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Regulation of gene expression: Prokaryotic
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... Structural insights into the function of the P-domains of lectin chaperones Authors: Kalle Gehring, Guennadi Kozlov ...
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... The IMGT/Collier-de-Perles [14] tool was created by LIGM (Université Montpellier 2, CNRS) and is part of IMGTW, the international ImMunoGeneTics information systemW [15,16] (IMGTW, http://www.imgt.org), which is acknowledged as the global reference in immunogenetics and immunoinformatics. IMGT/Colli ...
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... function. One viable approach to address proteopathies may be to direct these species for degradation, using endogenous cellular machineries. In mammalian cells, proteins with biosynthetic errors are mainly degraded using the ubiquitinproteasome system (UPS). In this study, we have applied intracell ...
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... increasingly resistant to a broad spectrum of antibiotics. New ways to combat these bacteria are needed. The Greenfield High School SMART (Students Modeling A Research Topic) Team is modeling the enzyme GatCAB using 3D printing technology. GatCAB is found in certain bacteria and archaea and could be ...
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... Report on the digestibility of hydrolysed feather protein. The trial was ordered and paid by Sonac BV, P.O. Box 47, 5690 AA Son, The Netherlands. The purpose of the trial was to measure the apparent mink digestibility of crude protein (CP) and amino acids in hydrolysed feather protein. Material and ...
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Membrane structure, I

... specific substances, even though those substances may not be very concentrated in the extracellular fluid. Embedded in the membrane are proteins with specific receptor sites exposed to the extracellular fluid. The receptor proteins are usually already clustered in regions of the membrane called coat ...
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Protein



Proteins (/ˈproʊˌtiːnz/ or /ˈproʊti.ɨnz/) are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within living organisms, including catalyzing metabolic reactions, DNA replication, responding to stimuli, 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 three-dimensional 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 about 20-30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues in a protein is defined by the sequence of a gene, which is encoded in the genetic code. In general, the genetic code specifies 20 standard amino acids; however, in certain organisms the genetic code can include selenocysteine and—in certain archaea—pyrrolysine. Shortly after or even during synthesis, the residues in a protein are often chemically modified by posttranslational modification, which alters the physical and chemical properties, folding, stability, activity, and ultimately, the function of the proteins. Sometimes proteins have non-peptide groups attached, which can be called prosthetic groups or cofactors. Proteins can also work together to achieve a particular function, and they often associate to form stable protein complexes.Once formed, proteins only exist for a certain period of time and are then degraded and recycled by the cell's machinery through the process of protein turnover. A protein's lifespan is measured in terms of its half-life and covers a wide range. They can exist for minutes or years with an average lifespan of 1–2 days in mammalian cells. Abnormal and or misfolded proteins are degraded more rapidly either due to being targeted for destruction or due to being unstable.Like other biological macromolecules such as polysaccharides and nucleic acids, proteins are essential parts of organisms and participate in virtually every process within cells. Many proteins are enzymes that catalyze biochemical reactions and are vital to metabolism. Proteins also have structural or mechanical functions, such as actin and myosin in muscle and the proteins in the cytoskeleton, which form a system of scaffolding that maintains cell shape. Other proteins are important in cell signaling, immune responses, cell adhesion, and the cell cycle. Proteins are also necessary in animals' diets, since animals cannot synthesize all the amino acids they need and must obtain essential amino acids from food. Through the process of digestion, animals break down ingested protein into free amino acids that are then used in metabolism.Proteins may be purified from other cellular components using a variety of techniques such as ultracentrifugation, precipitation, electrophoresis, and chromatography; the advent of genetic engineering has made possible a number of methods to facilitate purification. Methods commonly used to study protein structure and function include immunohistochemistry, site-directed mutagenesis, X-ray crystallography, nuclear magnetic resonance and mass spectrometry.
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