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Kojo Mensa-Wilmot* and Paul T.Englund Department of Biological
Kojo Mensa-Wilmot* and Paul T.Englund Department of Biological

... Blue/white color selection, based on insertional inactivation of /3-galactosidase (1), is a powerful tool for DNA cloning in E. coli. However, proteins expressed from such recombinants are fusion proteins. Although these are very valuable, non-fused proteins are much more desirable for many biochemi ...
PRESS RELEASE DNA repair: a new letter in the cell alphabet
PRESS RELEASE DNA repair: a new letter in the cell alphabet

... activate them and make them functional. They function as letters of a coding alphabet that the cell can use to determine what to do with a specific protein, for instance sending it off to the cell nucleus to repair damage to our genes. “We were investigating one of the most complex tags, which is kn ...
Chapter 3 Section 4 Protein Synthesis
Chapter 3 Section 4 Protein Synthesis

... • Transcription – the DNA strand is unzipped to allow a strand of mRNA to be created from its exposed nitrogen bases • The new strand of mRNA are made by matching new nitrogen bases with the exposed nitrogen bases from the unzipped strand of DNA. ...
Signaling Through Scaffold, Anchoring, and Adaptor Proteins
Signaling Through Scaffold, Anchoring, and Adaptor Proteins

... guanosine triphosphatases (GTPases), protein kinases, transcription factors, and polypeptides that regulate cytoskeletal architecture and cell adhesion. A genetic test of this concept has been provided in mice by use of the Met receptor tyrosine kinase, which has two closely spaced autophosphorylati ...
1. I can tell the difference between mRNA, tRNA, and rRNA
1. I can tell the difference between mRNA, tRNA, and rRNA

... nitrogen base Thymine (G = C, A = T), and is double stranded. It stays in the nucleus. RNA: Ribonucleic Acid is used in the process of building the proteins. RNA has the sugar ribose, contains the nitrogen base Uracil (G = C, A = U), and is single stranded. It can move from the nucleus into the cyto ...
Gene Section PA2G4 (proliferation associated 2G4, 38kDa) -
Gene Section PA2G4 (proliferation associated 2G4, 38kDa) -

... and Jost, 1995). The MW of this protein is predicted to be 38058 D, consisting of 340 amino acids. The human orthologue EBP1 was later identified as an ErbB3 binding protein of the same MW as the mouse protein (Yoo et al., 2000). This form migrates at approximately 42 kD in SDS-PAGE gels. Later, a l ...
What Triggers Inflammation?
What Triggers Inflammation?

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Proteomics - University of Warwick
Proteomics - University of Warwick

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Hidden Markov models for detecting remote protein homologies
Hidden Markov models for detecting remote protein homologies

... Homologs are chromosomes carrying the same genetic loci; a diploid cell has 2 copies of each homolog, one derived from each parent. A profile of a protein family is a labeling of the positions of the amino acids in the secondary structure and a probability distribution for each position. The stru ...
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Dynamical Analysis of Networks: How to Identify Important Nodes with

... Protein native structure ↔ energy minimum Protein dynamics ↔ shape of energy function ...
Chapter Fourteen Grading ~ Viruses
Chapter Fourteen Grading ~ Viruses

... ...
Summary of Endomembrane
Summary of Endomembrane

... group in a protein(Asp-X-Ser or Asp-x-Thr) are said to be N-linked oligosaccharide, common on glycoprotein. This occurs in RER, but futher modification hold on in Gol. O-linked: Sugars are covalently linked to the selected hydroxyl group of serine or threonine in a protein to form O-linked glycoprot ...
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High Protein Low-Glycemic Diets Better at Maintaining Weight Loss
High Protein Low-Glycemic Diets Better at Maintaining Weight Loss

... Five hundred forty-eight subjects completed six months on the assigned diets. In the analysis of participants who completed the study, only the low-protein/high-GI diet was associated with subsequent significant weight regain (1.67 kg, or 3.6 lbs) by the end of the dietary intervention. Weight regai ...
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Chapter 11 - GEOCITIES.ws

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Lipids and proteins Lipids:

... Like dissolves like: Organic compounds dissolve other organic compounds, while inorganic compounds dissolve inorganic compounds. - Lipid solubility: To 1ml oil on a test tube, add 2ml of ether, acetone, CCl4, alcohol & water separately, and then watch the result. ...
i) Suggest reagents and conditions for each step in the following
i) Suggest reagents and conditions for each step in the following

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Human BMF / Bcl2 modifying factor Protein (His Tag)
Human BMF / Bcl2 modifying factor Protein (His Tag)

... family members form hetero- or homodimers and act as anti- or proapoptotic regulators that are involved in a wide variety of cellular activities. BMF contains a single BCL2 homology domain 3 (BH3), and has been shown to bind BCL2 proteins and function as an apoptotic activator. BMF is found to be se ...
question #5
question #5

... proteins are made of amino acids and amino acids have nitrogen. Nucleic acids always contain nitrogen because nucleic acids consist of three parts, one of which is a nitrogen base. The other two parts are a sugar, which is made up of carbon, hydrogen, and oxygen, and a phosphate group, made up of ox ...
Fall 2010.pub - Body Symmetry
Fall 2010.pub - Body Symmetry

... Over the summer we hired a new trainer, Joy Guardia. Joy came to Body Symmetry with a lot of experience. She has worked as a personal trainer for several years in the Springfield community and is an avid runner, having competed at the collegiate level in women’s track and cross country for 4 years. ...
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... outside the cell activate a Ca2+ channel in the patch? •There can’t be a direct connection •There must be a mobile “second messenger” inside the cell ...
Disulphide-bond formation in protein folding catalysed by highly
Disulphide-bond formation in protein folding catalysed by highly

... The classic work on the refolding of reduced ribonuclease (see Anfinsen, 1973) showed that the fully reduced unfolded protein can regain the correctly disulphide-paired active conformation without the supply of additional information; however, rapid refolding requires the presence of a thiol-disulph ...
The Truth About Protein
The Truth About Protein

... Although protein supplements claim they have the important amino acids, they aren’t as plentiful as they would like you to think. Plus, in general, engineered foods don’t absorb as well and they lack beneficial nutrients. Stick to natural foods like cottage cheese, yogurt, lean meats, nuts, etc. Not ...
Efficacy of fungicide treatments on the winter wheat senescence
Efficacy of fungicide treatments on the winter wheat senescence

... weather conditions of the harvest year and on the F applied. F use prolonged retention of green canopy of wheat plants in 2003–2004. Chlorophyll concentrations in flag leaves at the end of plant vegetation, i. e. in the fifth week after F treatment, were higher in the plots treated with strobilurins ...
Outline - Membranes Membranes Membrane Phospholipids
Outline - Membranes Membranes Membrane Phospholipids

... protein triggers change back to original conformation, potassium moves into cell, and the cycle repeats. ...
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Protein phosphorylation



Protein phosphorylation is a post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or modifying its function. The reverse reaction of phosphorylation is called dephosphorylation, and is catalyzed by protein phosphatases. Protein kinases and phosphatases work independently and in a balance to regulate the function of proteins. The amino acids most commonly phosphorylated are serine, threonine, and tyrosine in eukaryotes, and histidine in prokaryotes, which play important and well-characterized roles in signaling pathways and metabolism. However, many other amino acids can also be phosphorylated, including arginine, lysine, and cysteine. Protein phosphorylation was first reported in 1906 by Phoebus Levene at the Rockefeller Institute for Medical Research with the discovery of phosphorylated vitellin. However, it was nearly 50 years until the enzymatic phosphorylation of proteins by protein kinases was discovered.
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