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Chapter 5 part II
Chapter 5 part II

... of glass slide or silicon chip. • The proteins arrayed can be antibodies specific for each protein in an organism, purified recombinant proteins, or short synthetic peptides. • There are many ways of attaching a protein to a support surface. • The major objective of any coupling system is maintenanc ...
The Synthetic Machinery of the Cell
The Synthetic Machinery of the Cell

... Barbiturates are a group of drugs that were used for the treatment of insomnia, as short-acting anaesthetics and for the treatment of epilepsy. Their use is now restricted because they induce dependence and have several undesirable side effects. Prolonged use of barbiturates induced proliferation of ...
Protein Synthesis PPT
Protein Synthesis PPT

... 3. RNA contains Uracil instead of Thymine 4. RNA is disposable 5. RNA can be outside the nucleus, DNA can’t If you are going from DNA to RNA – what nitrogenous base would pair with Adenine? DNA: C A G T T A RNA: _ _ _ _ _ _ ...
Answers for possible questions about the new material HbS·(O2)4 (aq)
Answers for possible questions about the new material HbS·(O2)4 (aq)

... cells, into the cytoplasm where the information can be translated into protein. Transfer RNA (tRNA) is the direct interpreter of genetic information found in mRNA into the sequence of amino acids for a protein using its three base anti-codon located at one end and attached amino acid at the other. R ...
Macromolecules - Essentials Education
Macromolecules - Essentials Education

... poypeptides usually make up a protein. They can also code for the production of an RNA molecule.   ...
Lecture 2 Protein conformation Recap Recap… Proteins
Lecture 2 Protein conformation Recap Recap… Proteins

... Carboxyl end (C-terminus) ...
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29 - Alamo Colleges

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The amino acids

... common that they have short side chains that can form hydrogen bonds with the own backbone. These hydrogen bonds compensate the energy loss caused by bending the chain into a ...
Titration analysis of UbcH5B upon complexation
Titration analysis of UbcH5B upon complexation

... observe peaks arising from every amide proton and the connected amide nitrogen. The nitrogens have to be of the 15N isotope for this NMR experiment; so one needs an 15N-labelled protein. An HSQC spectrum is like a nice "fingerprint" of the protein because each peak corresponds to an NH of each resid ...
Medical School Biochemistry - Fall 2002
Medical School Biochemistry - Fall 2002

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Chem*3560 Lecture 26: Cell adhesion and membrane fusion
Chem*3560 Lecture 26: Cell adhesion and membrane fusion

... binding proteins found on the plasma membrane surface. The extracellular structure consists of five consecutive β-sheet domains with Asp-rich junctions that bind Ca2+. Ca2+ ions can serve as bridges between two negative molecules, but β-sheets are also designed to pair up so that a cadherin only bin ...
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... amino acids which are L-isomers. ...
Diversity in biological molecules
Diversity in biological molecules

... every position in them is occupied by one of 20 amino acids. Comparisons of such structures lend themselves to computer analysis, and freely available software such as ClustalW2 (see Websites) can be used to line up a series of protein sequences to show which ones are most similar and, interestingly ...
Unfolded Protein Response (UPR)
Unfolded Protein Response (UPR)

... Isolation of yeast mutant which can not induce expression of BiP mRNA against misfolded protein accumulation in the ER. ...
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Translation Worksheet Answers Translation occurs when mRNA is

... A ribosome consists of two subunits; the large subunit and the small subunit. During translations mRNA resides between the two subunits. There are three sites for tRNA to enter and build a polypeptide chain. They are called; 1. A site (aminoacyl binding site) 2. P site (peptide binding site) 3. E si ...
Macromolecule Molecular Structure Carbohydrates
Macromolecule Molecular Structure Carbohydrates

... Proteins Continued Proteins arrange themselves first in chains, then in aÅ -helix, then in folded aÅ -helix and finally in a quaternary structure Primary Structure– ...
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... tRNA looped structure On one of its loops it carries a triplet of bases; anticodon One of its trailing end AA ( AA pool)is attached through high energy ester bond catalyzed by aminoacyl-tRNA synthetase tRNA transport AA to the correct site of mRNA on ribosome particles ...
WorkSheet_4ANS
WorkSheet_4ANS

... 1. Gastric HCl is responsible for the low pH <2 of gastric juice. 2. Gastric acid kills microorganisms and denatures dietary proteins preparing them for hydrolysis by proteases. 3. Gastric juices contain the acid stable proteases of the pepsin family, which produce large peptide fragments and some f ...
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3 types of protein transport

Post-translational modifications on human cell expressed
Post-translational modifications on human cell expressed

... MS methods such as MALDI-MS typically are not able to detect glycopeptides due to their very large mass. By removing the oligosaccharides not only does the chance of seeing the peptides increase, but also critical information can be obtained as to the sites of glycosylation. Removing the Nlinked oli ...
BioN03 Amino acids, peptides, proteins Summer 2015
BioN03 Amino acids, peptides, proteins Summer 2015

... With four different groups connected to the tetrahedral αcarbon atom, amino acids can be present in two forms that are mirror-images of each other (they are enantiomers). They are called L isomer and D isomer. Amino acids with their two isomers are said to be chiral (when a central carbon is bonded ...
Macromolecules in your Food! – Info Sheet
Macromolecules in your Food! – Info Sheet

... Protein is mainly found in the following foods: meats, poultry, and fish, legumes (dry beans and peas), tofu, eggs, nuts and seeds, milk and milk products, and grains. Most adults in the United States get more than enough protein to meet their needs. It is rare for someone who is healthy and eating ...
glossary of technical terms
glossary of technical terms

... non-Sanger-based high-throughput DNA sequencing technologies. Millions or billions of DNAs can be sequenced in parallel, yielding substantially more throughput for genome sequencing ...
Instructions for Gram-LocEN Web-server
Instructions for Gram-LocEN Web-server

... where most of the cellular activities, such as cell division and metabolic pathways, occur. Extracellular space refers to the space outside the plasma membrane, which is occupied by fluid. For Gram-negative bacteria species, their proteins are located in eight subcellular locations, including cell i ...
Topic 3
Topic 3

... Proteins – Molecules • Enzymes • Cytoskeletal elements • Receptors • Specialized transmembrane proteins – Control resting and action potentials It is estimated that there can be hundreds of billions of different types of proteins that can be made, and our best estimate is that there are roughly 100, ...
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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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