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Phylogenetics workshop
Phylogenetics workshop

... • Rate of substitution varies at different positions in an amino acid sequence. • A proportion of sequences are likely to be invariant, generally have an essential role in the function of a protein. • A gamma distribution models the variation of rates at different sites. • Sites are sorted into gamm ...
Substrate targeting mechanisms
Substrate targeting mechanisms

... 1) Catalytic switching mechanisms -the ability to switch on and off in response to specific upstream signals 2) Substrate targeting mechanisms - The ability to select a restricted set of substrates in the cell any one time -15,000+ proteins in the genome - each with many phosphorylatable sites (ser/ ...
Monomeric state and ligand binding of recombinant GABA transporter Xiao-Dan Li
Monomeric state and ligand binding of recombinant GABA transporter Xiao-Dan Li

... planar heterocyclic compounds without a carboxyl group [5]. Some of these inhibitors are also substrates for they can be translocated across the membrane by GabP under appropriate conditions [6]. E. coli GABA transporter is a member of the amino acid/ polyamine/organocation (APC) transporter superfa ...
Unit 3 - Madison Public Schools
Unit 3 - Madison Public Schools

... enzymes. Hydrogen peroxide (H2O2) is a natural by-product of cellular metabolism. Enzymes in peroxisomes break hydrogen peroxide into water and oxygen gas.  Prevalent in cells that are synthesizing and breaking down lipids.  In germinating seeds the peroxisomes break down fatty acids into sugars n ...
Macromolecules & Enzymes
Macromolecules & Enzymes

... Lipid units: 1 Glycerol and 3 Fatty Acids Hydrophobic and non-polar Functions: Insulation, membrane structures, hormones, padding and waterproof coverings. Saturated – no double bonds, solid animal fats Unsaturated – one double bond, oils (from plants) ...
Supplementary Information (doc 48K)
Supplementary Information (doc 48K)

... determined the accurate precursor masses for all peptide peaks using the entire LC elution ...
4.2.1 Amino acids booklet 2013
4.2.1 Amino acids booklet 2013

... b) One of you should now replace a hydrogen atom on the central carbon atom for a methyl group (you have made a new amino acid called alanine) and repeat the ...
Chapter 17
Chapter 17

Anti-Hepatitis C Virus Core Antigen antibody [1F6] (Biotin)
Anti-Hepatitis C Virus Core Antigen antibody [1F6] (Biotin)

... protein is thought to contribute to HCV pathogenesis through its interaction with various signal transduction pathways. In addition, HCV core antigen is a recently developed marker of hepatitis C infection. The HCV core protein has been previously shown to circulate in the bloodstream of HCV-infecte ...
sv-lncs - Department of Computer Science and Engineering
sv-lncs - Department of Computer Science and Engineering

... typically comprised of an intricate sequence involving a variation of twenty common amino acids, which are molecules that, in turn, consist of a single carbon molecule flanked by four different attached molecular functional groups. Proteins provide evidence for the occurrence of evolution and functi ...
3040 - Zhang, Hongyu
3040 - Zhang, Hongyu

... alternative conformations. This assumption has been demonstrated to be true by lots of experimental data, most famously the pioneering experiment of Christian Anfinsen (Voet & Voet, 1995). The attractiveness of the ab initio approach is that not only it promised to solve the protein structure predic ...
INTRODUCTION TO MYCOLOGY
INTRODUCTION TO MYCOLOGY

Transcriptional regulation is only half the story
Transcriptional regulation is only half the story

... mRNA structure, putative miRNA target sites, and the presence of upstream start codons. The authors observed a lognormal distribution of protein-per-mRNA ratios—suggesting that many impendent factors together contrive to determine translational efficiency and protein degradation rates. Some of the s ...
Sample Preparation Guidelines for 2
Sample Preparation Guidelines for 2

... Note: If samples contain components not compatible with DIGE experiment, remove these contaminants by protein precipitation. A number of 2D clean-up kits are commercially available. After protein clean-up, redissolve the protein pellet with a compatible lysis buffer. Be sure to make the final protei ...
Exploring a Protein Structure in the RCSB PDB: Major
Exploring a Protein Structure in the RCSB PDB: Major

... bonds are formed by oxidation of two specific sulfur-containing amino acids. Rotate the model to visualize these bonds closely. Describe what (if any) role these bonds play in holding the MHC structure together. ...
Ribosome binding site Polysomes (多聚核糖体)
Ribosome binding site Polysomes (多聚核糖体)

... • The signal sequence of secreted proteins causes the translating ribosome to bind factors that make the ribosome dock with a membrane and transfer the protein through the membrane as it is synthesized. Usually the signal sequence is then cleaved off by signal peptidase. ...
A Figure S7. A. Standard curve of actin quantification using silver
A Figure S7. A. Standard curve of actin quantification using silver

... Figure S7. A. Standard curve of actin quantification using silver staining. Actin standards were prepared by serial dilution and separated using SDS gel electrophoresis. Silver staining was carried out and band quantification was accomplished using the BioRad QuantityOne software. Linear regression ...
Mutations Practice
Mutations Practice

... is single stranded (one half of the ladder). At the ribosome, another type of RNA (tRNA) transfers amino acids from the cytoplasm to the growing amino acid chain at the ribosome. BUT, sometimes there are problems with the DNA molecule that result in a change ...
Mutation Activity - Northwest ISD Moodle
Mutation Activity - Northwest ISD Moodle

... is single stranded (one half of the ladder). At the ribosome, another type of RNA (tRNA) transfers amino acids from the cytoplasm to the growing amino acid chain at the ribosome. BUT, sometimes there are problems with the DNA molecule that result in a change ...
Cell cycle control by ubiquitylation
Cell cycle control by ubiquitylation

... B. The E3 mediates the transfer of ubiquitin from the E2 to the substrate protein by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. ...
Screening for novel snake venom toxins using protein chemistry and molecular biology.
Screening for novel snake venom toxins using protein chemistry and molecular biology.

... We have been involved in isolation and characterization of novel toxins from snake venoms and identified a number of new toxins that belong to known family of toxins, but with different biological properties. We have also identified a few new families of snake venom toxins. The new toxins include (a ...
Novel eukaryotic enzymes modifying cell
Novel eukaryotic enzymes modifying cell

... membrane-anchored cell-surface proteins, whose amino acid side-chains are subject to numerous post-translational modifications. These modifications include addition of extensive polysaccharide moieties to asparagine or serine/threonine side chains (N and O linked glycosylation respectively), sulfata ...
15 Tacks and a 4 Foot Toober
15 Tacks and a 4 Foot Toober

... • And pairing green tacks that form disulfide bonds, • And keeping all of the polar white tacks on the surface of the protein. After everyone has folded their toober as best they can, the teacher can point out: • Every toober had a different random sequence of tacks (amino acids) and therefore each ...
Bodyguards and assassins: Bcl-2 family proteins and apoptosis
Bodyguards and assassins: Bcl-2 family proteins and apoptosis

... Chronic lymphocytic leukaemia (CLL) is the most common B-cell malignancy in the Western world and exists as subtypes with very different clinical courses. CLL is generally described as a disease of failed apoptosis. Apoptosis resistance may stem from a combination of microenvironmental survival sign ...
Electrophoresis Chapter 10 +
Electrophoresis Chapter 10 +

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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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