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1MBO Lopez kin
1MBO Lopez kin

... function as a biological metal chelator16; 17. While there was considerable questioning early on about the physiological need for such an enzyme, it is now clear that chelatases and metal chaperones are key elements of biological systems18; 19; 20; 21; 22; 23. Ferrochelatases among all organisms are ...
mnw2yr_lec16_2004
mnw2yr_lec16_2004

... • 56% of proteins were correctly predicted to have more than one domain • 42% of predictions are within 20 residues of a true boundary • 49.9% (44.6%) correct boundary predictions per protein ...
The protein folding problem consists of two parts: 1)Creating a
The protein folding problem consists of two parts: 1)Creating a

... Here is the example of the ribonuclease inhibitor which again shows this double layer of hydrophobic residues. ...
BS2550 Lecture Notes cAMP
BS2550 Lecture Notes cAMP

... inactivated by heating or NEM treatment; when these extracts are added to the (cyc-) membranes, you also get restoration of hormone sensitivity! The explanation for this apparent discrepancy is not that it is AC which is missing in the (cyc-) cells but another protein component, which was subsequent ...
supporting information file s1
supporting information file s1

... CoaE. In order to aid the selection of modeling templates for the N- and C-terminal domains of the mycobacterial CoaE, the Sequence Feature Scan tool from the Swiss-Model server which helps predict the secondary structure, presence of disordered regions and helps assign domains in the target sequen ...
Ch 14 Env Health 2013 - Pendleton
Ch 14 Env Health 2013 - Pendleton

... Smallpox, chicken pox ...
Chemistry Membranes Transport across membrane
Chemistry Membranes Transport across membrane

... the intracellular side of the plasma membrane of many cell types (e.g.erythrocytes). Mutations in spectrin cause hereditary defects of the erythrocyte. ...
Chemistry Membranes Transport across membrane
Chemistry Membranes Transport across membrane

... Peptides = oligopeptide (oligo = "few") formed from small number of amino acids (3-40), dipeptide, tripeptide, nonapeptide Proteins = polypeptide (poly = "many") are long, formed from hundreds to thousands - usually 300 amino acids (size is around ...
Sample Posters
Sample Posters

... NIH estimates that 23 million Americans have diabetes, and 6.2 million are undiagnosed. If untreated, diabetes can cause complications, including heart disease and neuropathy. Type II diabetes patients cannot regulate glucose due to insulin resistance or deficiency. Pyruvate carboxylase (PC) plays a ...
C483 Exam I 2014 Answer Key
C483 Exam I 2014 Answer Key

... ___F___ After a protein is denatured with denaturing agents, it cannot be renatured. ___F____ The tertiary structure of a protein may be formed from the folding of independent subunits to form a homodimer. ___T____Beta sandwiches are held together by hydrophobic forces. 10. (2pts each, 20 pts total) ...
Lecture 3a - Membs and Transport
Lecture 3a - Membs and Transport

... Note: even though a channel is required, this is still a passive process. Diffusion, by definition, is always passive. ...
MASE1 and MASE2: Two Novel Integral Membrane Sensory Domains
MASE1 and MASE2: Two Novel Integral Membrane Sensory Domains

... al., 2003]. An important feature of all those domains is their propensity to associate with more than one type of signal output domains (histidine kinases, adenylate cyclases, chemotaxis transducers), which made possible their recognition as conserved domains. In addition, these domains are often fo ...
COMPARATIVE MODELING AND MOLECULAR
COMPARATIVE MODELING AND MOLECULAR

... In silico-developed homology protein structure modeling builds a threedimensional model of a given protein sequence based on its similarity to one or more known structures belonging to the same member of a protein family. The purpose of this study is strongly related to a drug discovery strategy aga ...
13765_2016_148_MOESM1_ESM
13765_2016_148_MOESM1_ESM

... Fig. 1 (A) Binding model of compound 3c into E. coli FabH (Protein Data Bank entry: 1HNJ). The green dotted lines show the hydrogen bond, the blue dotted lines show -alkyl interactions, and the yellow dotted lines show -sulfur interactions. (B) 2D ligand interaction diagram with E. coli FabH using ...
12010_2017_2424_MOESM1_ESM
12010_2017_2424_MOESM1_ESM

... R192K mutation is the next important and common mutation found in all the mutant enzymes under consideration. Amino acid at position 192 is present at the entrance of the active site of enzyme through which the substrate molecules enter into the active site cavity of the enzyme. Supplementary Fig 4 ...
Prediction of protein disorder: basic concepts and practical hints
Prediction of protein disorder: basic concepts and practical hints

... putative domains (GlobDom) ...
Final Examination
Final Examination

... 27. [5 points] In a protein there is an alpha-helix composed of 11 amino acyl residues. In the folded protein, this alpha-helix lays next to a flat region of a beta-sheet that has hydrophobic amino acids on the surface nearest the alpha-helix. The other side of the alpha-helix is exposed to solvent ...
Slide 1
Slide 1

... •Incorporates distinct HMM models for signal peptides and TM helices •Signal peptide sequence ignored •Can use sequence homologs and multiply aligned sequences ...
Solutions to 7
Solutions to 7

... Of the possible orientations for Minoxidil in the binding site, only one orientation is consistent with the results above. Please check your model carefully, revise it if needed and answer the following questions. In the model proposed here, the important features are the hydrogen bonding of Minoxid ...
Globular Protein Structure
Globular Protein Structure

... The basic functional unit of protein tertiary structure is the domain. In its basic form, a domain is a structurally or functionally distinct parts of the protein. Small globular proteins (e.g., ribonuclease A) usually have only one domain whereas larger proteins (remember proteins can have molecula ...
Proteins in Solution and in Membrane
Proteins in Solution and in Membrane

... • Porin proteins are trimeric, a group of 3 beta-barrels. • Has a 16-stranded beta-barrel structure • Core of barrel has narrow aqueous channel. • Porins are unusual membrane proteins in not very hydrophobic and in being composed of beta structure • Small molecules with MW less than about 600 can pa ...
Coming Soon !!! The next lecture will review step 4 and cover this as
Coming Soon !!! The next lecture will review step 4 and cover this as

... 5- Look for signatures of protein-protein interactions and use these to guide docking together of the different subunits or domains of the complex (Quaternary structure). In our case we are just reconstructing a single protein, but have only found structural templates for two separate portions of th ...
Toxic shock syndrome toxin-1 from Staphylococcus aureus Product
Toxic shock syndrome toxin-1 from Staphylococcus aureus Product

... from pH 2.5-11 and at temperatures exceeding 60 °C. In its active form, TSST-1 contains 194 amino acid residues and has a molecular weight of approximately ...
Solution Structure of Choline Binding Protein A of Streptococcus
Solution Structure of Choline Binding Protein A of Streptococcus

... exhibits a typical R1 domain but lacks a complete R2 domain. However, a segment of this sequence is 85% identical to the Helix 1 and Helix 2 segment of domain R2 of CbpA-TIGR4, including the conserved residues illustrated in Fig. 1C. PspC 6.14 (Group 6) exhibits a single R2like domain while PspC 6.4 ...
5IntracellTrans
5IntracellTrans

... B. The protein eventually will move through the vesicular pathway. C. This occurs when proteins are transported into chloroplasts and mitochondria. D. The signal peptide is cleaved after the protein enters its target destination. E. transport requires the action of a “membrane transport complex.” 2. ...
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Anthrax toxin



Anthrax toxin is a three-protein exotoxin secreted by virulent strains of the bacterium, Bacillus anthracis—the causative agent of anthrax. The toxin was first discovered by Harry Smith in 1954. Anthrax toxin is composed of a cell-binding protein, known as protective antigen (PA), and two enzyme components, called edema factor (EF) and lethal factor (LF). These three protein components act together to impart their physiological effects. Assembled complexes containing the toxin components are endocytosed. In the endosome, the enzymatic components of the toxin translocate into the cytoplasm of a target cell. Once in the cytosol, the enzymatic components of the toxin disrupts various immune cell functions, namely cellular signaling and cell migration. The toxin may even induce cell lysis, as is observed for macrophage cells. Anthrax toxin allows the bacteria to evade the immune system, proliferate, and ultimately kill the host animal. Research on anthrax toxin also provides insight into the generation of macromolecular assemblies, and on protein translocation, pore formation, endocytosis, and other biochemical processes.
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