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Untitled
Untitled

... machine made up of RNA and protein, called the ribosome. The ribosome is able to catalyze the polymerization of a protein chain at the rate of up to five amino acids per second. Small proteins of 100 – 200 amino acids are therefore made in a minute or less. ...
PROTEIN SYNTHESIS
PROTEIN SYNTHESIS

... 2) The ternary complex binds to the 40S ribosome subunit. 3) Ribosomal 40S subunit binds to a complex of proteins at the 5’ end of capped mRNA. -Almost all eukaryotic mRNAs are capped, i.e. contain an inverted 7MethylGTP (m7GTP) attached to the first nucleotide. -The cap is a signal to ribosomes tha ...
Unit 3 PP - shscience.net
Unit 3 PP - shscience.net

...  Vitamin D (bones)  Vitamin C (immune) ...
peptides - WordPress.com
peptides - WordPress.com

... Digestion ...
N-Methylated Amino Acids
N-Methylated Amino Acids

Protein-nucleic acid interactions
Protein-nucleic acid interactions

... Zipper-type proteins — The leucine zipper (bZIP) contains an a-helix with a leucine at every 7th amino acid. The leucines act as the teeth of a zipper that allows dimerization of two proteins. Basic amino acids bind to the sugar-phosphate backbone while the helices fit in the major grooves on opposi ...
Complete nucleotide sequence of RNA 4 of rice stripe virus isolate T
Complete nucleotide sequence of RNA 4 of rice stripe virus isolate T

... plants produce peptides of different Mrs. Recently, three ...
- Wiley Online Library
- Wiley Online Library

... their virulence proteins with several functions led to the hypothesis that the VirE2 protein may have an additional function. Several experimental results now show this to be the case. As the VirE2 protein had been found in the membrane fractions of Agrobacterium [9], the possibility that the VirE2 ...
Amino Acids: An Introduction to Their Structure, Functions and
Amino Acids: An Introduction to Their Structure, Functions and

... group replacing a –H (Images at bottom left and right of previous page). As a rule, ser has a function similar to that of threonine (thr; images left and right), another hydroxylated amino acid: it serves as an activation site in enzymes, i.e., when it is phosphorylated or dephosphorylated, the enzy ...
nerve agents - 20 Years of OPCW
nerve agents - 20 Years of OPCW

... This is especially the case of hydrophilic agents such as Sarin while lipophilic agents such as VX can form depots of intact agent in fatty tissues. In case of Sarin the primary hydrolysis product (which is unable to block AChE) is isopropyl methylphosphonic acid (IMPA) that can further degrade to m ...
Chapter 27 - Extras Springer
Chapter 27 - Extras Springer

... Net protein synthesis is higher with casein protein than with soy protein. Casein protein has a higher biological value because the slow release property keeps the amino acids from being released rapidly and degraded in the liver into urea (Luiking, Deutz, Jake, et al., 2005). Whey protein is consid ...
Chemical Analysis in the New Zealand Dairy Industry
Chemical Analysis in the New Zealand Dairy Industry

... Any dairy product is a variable mixture of a large number of different chemical species, which are usually grouped together into broad classes such as moisture, fat, protein (defined as (protein nitrogen (N) + non-protein nitrogen (NPN)) ! 6.38), anhydrous lactose and mineral salts (which includes c ...
калориметрическое исследование взаимодействия анионитов с
калориметрическое исследование взаимодействия анионитов с

... The questions connected with use of ion exchangers for extraction and division of amino acids are actual. As objects of research have been chosen strong-based anion exchangers: gel AB-17-8, АРА-1п and macroporous АВ-29-12П. Anion exchangers were in ОН–-form. For research used glycine (Gly), glutamic ...
1 A Comparative, Double-blind, Triple Crossover Net Nitrogen
1 A Comparative, Double-blind, Triple Crossover Net Nitrogen

... total consumption of each designated portion was reached. ...
Chapter 3
Chapter 3

... lipids with a variety of functions  Phospholipids are structurally similar to fats and are an important component of all cells – For example, they are a major part of cell membranes, in which they cluster into a bilayer of phospholipids – The hydrophilic heads are in contact with the water of the e ...
translation and protein structure
translation and protein structure

... folded proteins, where they are kept away from water. Amino acids with polar side chains have a permanent charge separation, in which one end of the side chain is slightly more negatively charged than the other. As we saw in Chapter 2, polar molecules are hydrophilic, and they tend to form hydrogen ...
occasional article intracellular protein degradation: from a vague
occasional article intracellular protein degradation: from a vague

... endosomes and phagocytic vacuoles (heterophagic vacuoles) that contain extracellular contents/particles; and multivesicular bodies (MVBs) which are the transition vacuoles between endosomes/phagocytic vacuoles and the digestive lysosomes. The discovery of the lysosome along with independent experime ...
The Methylosome, a 20S Complex Containing JBP1 and pICln
The Methylosome, a 20S Complex Containing JBP1 and pICln

... (33), anti-JBP1 (a kind gift from Michael Nunn and Gary Zieve), nonimmune antibody SP2/0 (12), and anti-Flag (Sigma). Immunoprecipitation on anti-Flag beads and elution with Flag peptide (Sigma) were done according to the manufacturer’s recommendation. Mass spectrometric identification of JBP1. The ...
Struct Bio 101
Struct Bio 101

... A single molecule is a very weak scatterer of X-rays. Most of the X-rays will pass through the molecule without being diffracted. Those rays which are diffracted are too weak to be detected. Solution: Analyzing diffraction from crystals instead of single molecules. A crystal is made of a three-dimen ...
A role of SAND-family proteins in endocytosis
A role of SAND-family proteins in endocytosis

... cells residing in the worm’s body cavity, called coelomocytes [cup (coelomocyte uptake defective) screen]. Yolk uptake by maturing oocytes is an example of the receptor-mediated endocytosis pathway in many species. Yolk storage vesicles are thought to be the oocyte equivalent of late endosomes or ly ...
Penicillin - Stephen F. Austin State University
Penicillin - Stephen F. Austin State University

... change shape and grow into long filaments. As the dosage is increased, the cell surface loses its integrity, as it puffs, swells, and ultimately ruptures. Penicillin attacks enzymes that build a strong network of carbohydrate and protein chains, called peptidoglycan, that braces the outside of bacte ...
PowerPoint Learning Quest
PowerPoint Learning Quest

... structure of cells because they make up the cell membrane’s of animal cells. As a result of these phospholipids, the cell membrane becomes selectively permeable, meaning that the cell can now regulate the passage of materials into and out of the cell’s interior. Cell (Plasma) Membrane Structure ...
Protein
Protein

... peptidases digest all the remaining dipeptides and tripeptides into individual amino acids for absorption into the bloodstream. Undigested protein Any parts of proteins that are not digested and absorbed in the small intestine continue on through the large intestine. People with celiac disease, for ...
Mutants of the Membrane-binding Region of Semliki Forest Virus E2
Mutants of the Membrane-binding Region of Semliki Forest Virus E2

... (COOH-terminal). This chimera had the topology predicted by the stop transfer postulate. We decided to study the features of the membrane-binding region of a group I polypeptide that are important for its function using the extremely powerful approach of in vitro mutagenesis followed by in vivo expr ...
Document
Document

... catalyst to speed up chemical reactions • Enzymes can perform their functions repeatedly, functioning as workhorses that carry out the processes of life ...
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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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