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Normal Protein Trafficking and the Unfolded Protein Response
Normal Protein Trafficking and the Unfolded Protein Response

... protein response is triggered. During the unfolded protein response cells may respond by: • destroying the proteins • trying to refold the proteins • commit apoptosis (cell suicide) ...
PTM
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... • Glutamine synthetase is adenylylated (i.e. AMP is added) at a specific tyrosine residue. The enzyme is inactive when it is adenylylated. The degree of adenylylation is controlled by a regulatory protein, PII. • The ability of PII to regulate the adenylylation of glutamine synthetase is in turn reg ...
Cell cycle control by ubiquitylation
Cell cycle control by ubiquitylation

... Rbx1, which contains the RING domain, and Cul1 form a catalytic core complex that recruits a cognate E2 F-box proteins are characterized by an amino-terminal 40-residue F-box motif that binds Skp1 followed by protein–protein interaction modules such as leucine ...
Building proteins
Building proteins

... Why organelles? Specialized structures specialized functions cilia or flagella for locomotion Containers partition cell into compartments create different local environments separate pH, or concentration of materials distinct & incompatible functions lysosome & its digestive enzymes Membranes as sit ...
Structure Reveals How Cells `Sugar
Structure Reveals How Cells `Sugar

... Biologists at the U.S. Department of Energy's Brookhaven National Laboratory, Stony Brook University, and the University of Wurzburg, Germany, have deciphered the structure of a large protein complex responsible for adding sugar molecules to newly formed proteins - a process essential to many protei ...
Protein Misfolding and Degenerative Diseases
Protein Misfolding and Degenerative Diseases

... Biochemistry is the science that studies the chemical processes in living organisms. Using different experimental models, biochemists demonstrated that most of the cell's chemical reactions and structural components are mediated or supplied by proteins. These experiments revealed that proteins are c ...
CH 107 SI Summer 2015 Worksheet 13 Answers What are the two
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... 1. What are the two major types of secondary protein structure and what bonds are present in each? α-helices and β-sheets Hydrogen bonds 2. What types of interactions can be present in tertiary protein structure? Rank the interactions from strongest to weakest. disulfide bonds >> salt bridges > hydr ...


... Phone: +46 8 673 95 00, Fax: +46 8 15 56 70, E-mail: [email protected], Website: www.kva.se ...
The Chemicals of Life
The Chemicals of Life

... Base element for many macromolecules in the body Carbon is a small element that can form 4 stable covalent bonds with other atoms (look at valence electrons). The number of covalent bonds an atom can form is called its bonding capacity. Carbon can bond to other carbon atoms in straight chains, branc ...
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... How will a persistent reduction of the [Na+] outside a neuron affect the amplitude of the action potentials? A) The amplitude will be increased. B) The amplitude will be decreased. C) The amplitude will be unchanged. D) The amplitude will first increase and then decrease. E) The amplitude will first ...
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... of peptides and proteins. Background material in basic protein chemistry will be provided along with a review of mass analyzers, acquisition types, and ionization sources used for protein and peptide analysis. Real-world examples will be used to illustrate protein sample preparation strategies, char ...
Death or Damage of Dopamine neurons
Death or Damage of Dopamine neurons

... movement, cognition, learning, and mood, explaining the dementia and difficulty with motor control exhibited by patients with deficits in the production of this key neurotransmitter. The a-synuclein gene was one of the first to be implicated in this disease. It produces a protein that can, in certai ...
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Protein Folding and Membrane Structure

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... the researchers mimicked these mechanisms in somatic tissues of model organisms to extend lifespan and delay age-related diseases. Their research was published in Nature Communications on November 28. The survival of an organism is linked to its ability to maintain the quality of the cellular protei ...
The Cold Never Bothered Me Anyway Measuring the Forces at Work
The Cold Never Bothered Me Anyway Measuring the Forces at Work

... temperature and is thought to help maintain protein production. It has a highly conserved structure but small differences in the amino acid sequence of extremophilic Cold Shock proteins change their flexibility, allowing them to move about and operate at the environment temperature of the organism. ...
CRYSTAL 24 Abstract Submission Form
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... series of mutant proteins that have enhanced activity towards the non-physiological substrates, -naphthyl acetate and p-nitrophenyl acetate. In terms of steady state kinetics, the mutations caused a drop in the Km for the hydrolysis reaction with these two substrates. For the best mutant, there was ...
Fates of Proteins in Cells
Fates of Proteins in Cells

... lumen, it gets glycosylated at sites called sequons, determined by particular protein sequence details. For example, an asparagine (N) will be glycosylated, if it is part of a sequon pattern -N-X-S- or -N-XT- where X is any amino acid, S is serine and T is threonine, so long as X is not P (proline). ...
Protein Degradation, Volume 1 ch01_p 1..9
Protein Degradation, Volume 1 ch01_p 1..9

... the aim of isolating its components and characterizing their mode of action. In this work, I was greatly helped by Aaron Ciechanover, who was my graduate student at that time. I have also received a lot of support, help, and great advice from Irwin Rose, in whose laboratory at Fox Chase Cancer Cente ...
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... growth factor (HGF), platelet derived growth factor (PDGF), and c-Kit receptors. Also known as Ruk (regulator of ubiquitous kinase) and SETA (SH3 domain-containing gene expressed in tumorigenic astrocytes), CIN85 is an ubiquitously expressed adaptor protein with three SH3 domains. It interacts with ...
Bacterial Cell Walls Contain Peptidoglycans
Bacterial Cell Walls Contain Peptidoglycans

... • Others are not dependent on glycans • Some are glycan-dependent in one cell type but not in another • Some glycosylation sites are more important than others – Aid in certain sorting events • In later secretory pathway of glycoproteins in Golgi – Structural features of glycans act as destination l ...
Polypeptide: alpha-helix and beta
Polypeptide: alpha-helix and beta

... Concept: Peptide chains tend to form orderly hydrogen-bonded arrangements. Materials:  alpha-helix and beta-sheet models made by Prof. Ewing Procedure: Models may be used to help explain secondary protein structure. Related Information: Fibrous proteins are stringy, tough, and usually insoluble in ...
Abstracts
Abstracts

... in neuroscience. Neurons are highly polarized cells—a long extended axon sends to, and elaborate dendrites receive signals from, neighbor neurons via the structure called synapse. Many proteins, such as neurotransmitter receptors and ion channels, need to be differentially sorted and trafficked to a ...
Just as 26 letters of the alphabet make up all words in the English
Just as 26 letters of the alphabet make up all words in the English

... language, 20 amino acids make up all of the proteins in your body. The structure of a protein is determined by the order of its amino acids. If two amino acids change places, the entire protein changes. The function of a protein depends on its structure. There are at least 100,000 proteins in your b ...
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Proteasome



Proteasomes are protein complexes inside all eukaryotes and archaea, and in some bacteria. The main function of the proteasome is to degrade unneeded or damaged proteins by proteolysis, a chemical reaction that breaks peptide bonds.
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