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5 nm Ni-NTA-Nanogold
5 nm Ni-NTA-Nanogold

... This product is supplied as a dark red colored liquid at a concentration of 0.5 µM in 50 mM MOPS, pH 7.9. No additional stabilizer or preservative is included. If a sterile solution is needed, filter the product with a 0.2 µm cellulose acetate membrane filter. As supplied, this product is stable at ...
Macromolecules
Macromolecules

... – If see-thru, it contains lipids ...
Macromolecules
Macromolecules

... – If see-thru, it contains lipids ...
NAME:
NAME:

... Gelatin is a protein made from collagen. Proteins are a basic type of matter that make up all living things. Collagen is a structural protein found in all animals, that helps give animals their structure, or shape. Collagen can be found in many parts of your body, including your skin, bones, muscles ...
Proteins
Proteins

...  Software used to generate theoretical peptide mass fingerprint (PMF) for all proteins in database  Match of experimental readout to database PMF allows researchers to identify the protein ...
B-PERfusions
B-PERfusions

... B-PER and fusion proteins time the pellets were uniformly dispersed in the lysis solution. From this point, the IPIII-His and MBP fusion lysates were processed differently, as detailed in the next two paragraphs. Purification of His-tagged fusion proteins To each IPIII-His fusion lysate was added 1 ...
Lecture #2 – Review of Protein Chemistry, Enzyme Specificity
Lecture #2 – Review of Protein Chemistry, Enzyme Specificity

... The various forces that are involved in establishing the structure of enzymes are also clearly involved in determining their specificity (ie, ionic interactions with trypsin, hydrophobic interactions with chymotrypsin and elastase). Only substrates that will fit into the binding pocket can be effect ...
Tertiary Structure
Tertiary Structure

... 1). Secondary structures are arranged in a few common patterns - i.e, resulting in protein “families”. 2). Proteins fold to form the most stable structure. Stability arises from: formation of large number of intramolecular hydrogen bonds reduction in hydrophobic surface area from solvent ...
Heat Shock Proteins and Neurodegenerative Disorders
Heat Shock Proteins and Neurodegenerative Disorders

... Heat shock proteins (HSPs), also known as stress proteins, were first discovered in 1962 by Ritossa[1], who observed that a transient increase in temperature induced puffing patterns in the chromosomes of salivary glands of Drosophila melanogaster larvae. Temperature increases were subsequently foun ...
Title New tricks for KDEL receptors Author(s)
Title New tricks for KDEL receptors Author(s)

... virus (DENV) secretion [5]. DENV is responsible for 50-100 million infections annually in over 100 endemic countries [6]. Viral particles assemble and bud into the ER lumen, translocate to the Golgi to complete their maturation and are released by exocytosis. During infection there is a massive over ...
Poster
Poster

... area has 40% alpha helixes and 3% beta sheets in its normal form. In the misfolded prion form, the area forms more beta sheets and then can bind to other normal molecules, causing them to misfold. •In yeast, the spread of prions is not genetic, but prions are passed from one generation of yeast to t ...
Renaturation of telomere-binding proteins after the fractionation by
Renaturation of telomere-binding proteins after the fractionation by

... if large number of gel slices have to be handled. However, there is a simpler method, described by Ossipow et al. (1993), which is based on the observation that mild non-ionic detergents, such as Triton X-100, remove SDS from protein-SDS complexes and sequester it into micelles that do not interfere ...
Expediting Purification of Cellular Proteins
Expediting Purification of Cellular Proteins

... from focusing on small numbers of molecules or cellular events to global functional analysis, feeding these results into new approaches for the prevention, diagnosis, and treatment of cancer. Methods that allow researchers to look across a broader angle at cellular processes such as mRNA expression ...
Anti-AP2M1 monoclonal antibody, clone 2D23
Anti-AP2M1 monoclonal antibody, clone 2D23

... surrrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directl ...
DNA/Protein structure-function analysis and prediction - IBIVU
DNA/Protein structure-function analysis and prediction - IBIVU

... 3D domain swapping definitions. A: Closed monomers are comprised of tertiary or secondary structural domains (represented by a circle and square) linked by polypeptide linkers (hinge loops). The interface between domains in the closed monomer is referred to as the C- (closed) interface. Closed monom ...
Chemical biology beyond binary codes
Chemical biology beyond binary codes

... dimer of the Phe36Met mutant and most interestingly, the interaction is between one of the `effector' loops (necessary for binding to the FK506^FKBP12 target calcineurin) and the FK506 binding site [1]. The FKBP-Met36 mutant could be used in an alternative, negative dimerization system, complementar ...
Biotransformation Problem Statement - ACE
Biotransformation Problem Statement - ACE

... using cationic cofactors are unable to perform reverse hydrolysis. Using a third party specialist to generate novel recombinant proteins, we are developing a small collection of alternative enzymes. Substrate specificity of phosphatases may be very diverse, as recently established for the hydrolysis ...
Proteomics studies of post-translational modifications in plants
Proteomics studies of post-translational modifications in plants

... pathogen treatment, a suspension culture of Arabidopsis was pulse-labelled with 32P and the phosphorylated proteins were visualized by 2DE. One of these proteins, AtPhos43, that was phosphorylated within minutes after treatment with flagellin or chitin fragments was identified by nanoESI MS/MS (Peck ...
Lost in translation - Botany - LMU Munich
Lost in translation - Botany - LMU Munich

... several components of the HSP90 machinery, which can also be linked to chloroplast preprotein import. In one study, a large set of wheat germ-translated chloroplast preproteins were analysed with respect to chaperone Wild type (right) and kinase mutant plants (left) during greening (top) and under n ...
Protein Synthesis and Degradation
Protein Synthesis and Degradation

... We describe the crystal structure of the complete Thermus thermophilus 70S ribosome containing bound mRNA and tRNAs at 5.5 A resolution. All of the 16S, 23S and 5S rRNA chains, the A-, P- and E-site tRNAs, and most of the ribosomal proteins can be fitted to the electron density map. The core of the ...
Slide 1
Slide 1

... Most of the proteins should fold in order to function Misfolding cause some diseases. Cystic Fibrosis ,affects lungs and digestive system and cause early death Alzheimers’s and Parkinson's disease It may help us to understand the structure of proteins which has not been known ...
ribosomes - Mircea Leabu
ribosomes - Mircea Leabu

... - small HSP (sHSP) - HSP40 - HSP60 - HSP70 - HSP90 - HSP100 Various mechanisms of action ...
biochem ch 37 [2-9
biochem ch 37 [2-9

... o Often, target protein is polyubiquitinylated (additional ubiquitin molecules added to previous ubiquitin molecules, forming long ubiquitin tail on target protein) o After polyubiquitinylation complete, targeted protein released from 3-enzyme complex and directed to proteasome via variety of mechan ...
Homeostasis External vs. Internal conditions
Homeostasis External vs. Internal conditions

... • Intron-exon system – one gene can produce multiple proteins through different splicing (alternative splicing) ...
word
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... Structural insights into the function of the P-domains of lectin chaperones Authors: Kalle Gehring, Guennadi Kozlov ...
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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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