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Proteins
We generally tend to think of proteins only from a dietary lens, as a component of what we eat. However, they are among the most important and abundant organic macromolecules in the human body, with diverse structures and functions. Every cell contains thousands and thousands of proteins, each with specific functions. Some help in the formation of cellular membrane or walls, some help the cell to move, others act as messages or signals and flow seamlessly from one cell to another, carrying information.
Protein Expression
The method by which living organisms synthesize proteins and further modify and regulate them is called protein expression. Protein expression plays a significant role in several types of research and is highly utilized in molecular biology, biochemistry, and protein research laboratories.
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- Under the microscope, the fluorescent signal from an isolated quantum point will form a stain: A.Approximately the same size as a fluorescent protein of the same colourB.Much smaller than a fluorescent protein, regardless of colourC.Relatively dark compared to antibodyD.Which corresponds approximately to the size of the quantum point, 20 to 40nm.You are studying the binding of proteins to thecytoplasmic face of cultured neuroblastoma cells andhave found a method that gives a good yield of inside-outvesicles from the plasma membrane. Unfortunately, yourpreparations are contaminated with variable amounts ofright-side-out vesicles. Nothing you have tried avoids thisproblem. A friend suggests that you pass your vesicles overan affinity column made of lectin coupled to solid beads.What is the point of your friend’s suggestion?. Our immune system makes many different proteins thatprotect us from viral and bacterial infection. Biotechnologycompanies must produce large quantities of these immune proteins for human testing and eventual sale to thepublic. To this end, their scientists engineer bacterial orhuman cell cultures to express these immune proteins.Explain why proteins isolated from bacterial cultures areoften inactive, whereas the same proteins isolated fromhuman cell cultures are active (functional).
- Predict the number of bands and apparent mol. wt. of the following proteins on SDS gels. 1. Immunoglobulin G in a reducing gel (β-mercaptoethanol added in the sample solution) – the light chains have a molecular weight of 25,000 Da and the heavy chains 50,000 Da.Predict the number of bands and apparent mol. wt. of the following proteins on SDS gels. 1. Immunoglobulin G in a non-reducing gel (no β-mercaptoethanol added in the sample solution) – the light chains have a molecular weight of 25,000 Da and the heavy chains 50,000 Da.Mild, non-ionic detergents (like Triton X-100, with polar but uncharged regions that do not denatureproteins) would be required for separation of which of the following proteins from cell membranes?A. monolayer-associated proteinsB. lipid-linked proteinsC. transmembrane proteinsD. integral proteinsE. peripheral proteins
- Design an assay with purified phycocyanin to test protein stability using 500ml of 95% ethanol. Then do the same with 2 M sodium chloride. Make each step clear.Consider the following properties of the protein components of a sample mixture as provided in the table below: 1. if the mixture is subjected to gel filtration chromotography which protein component elute first? 2. if the mixture is subjected to isoelectric focusing which protein will stop m oving nearest to the positive electrode? 3. if the mixture is subjected to cation-exchange chromotography using a buffer at ph 7 which protein will bind to the resin? 4.if the mixture is subjected to SDS-PAGE which protein will be at bottomost portion of gel? 5.if the mixture is subjected to hydrophobic interaction chromotography which protein will bind most strongly to the resin?α-Bungarotoxin is a powerful neurotoxin found in the venom of a poisonous snake (Bungarus multicinctus). It binds with high specificity to the acetylcholine receptor (AChR; an integral membrane protein) andprevents its ion channel from opening. This interaction was used to purify AChR from the electric organ of torpedo fish.(a) Outline a strategy for using α-bungarotoxin covalently bound to chromatography beads to purify the AChR protein. (b) Outline a strategy for the use of [125I]α-bungarotoxin to purify the AChR protein.
- Explain what the meaning of these distances is (e.g., from where to where?)Crystal structure of human monocyte chemotactic protein-2An antibody binds to another protein with anequilibrium constant, K, of 5 × 109 M–1. When it binds toa second, related protein, it forms three fewer hydrogenbonds, reducing its binding affinity by 11.9 kJ/mole. Whatis the K for its binding to the second protein? (Free-energychange is related to the equilibrium constant by the equa-tion ΔG° = –2.3 RT log K, where R is 8.3 × 10–3 kJ/(mole K)and T is 310 K.)SDS is a __________ that gives proteins a _____________ charge while SDS-PAGE separates proteins based upon their ___________. -chemical, negative, molecular mass -chemical, negative, charge -chemical, positive, charge How would you prepare 40 mL of a 1: 8,000 dilution of the antibody in a single step? a. 5 mL antibody added to 40 mL of TBST b. 8 mL antibody added to 40 mL of TBST c. 200μL antibody added to 40 mL of TBST d. 5μL antibody added to 40 mL of TBST On which molecule would you find an epitope? -antigen -antibody -dna polymerase -restriction enzyme In the Western blot performed, which of the following proteins is recognized by the primary (1st) antibody? a. BSA b. goat anti-rabbit c. rabbit anti-BSA Insufficient washing of the membrane during the immunodetection will cause weak or no signal from the blot. TRUE OR FALSE An agarose gel requires a specific orientation on the gel box in order to be poured. TRUE OR FALSE