What are the molecular weights of the protein X polypeptides? (pick 1 only) - 50 kDa each - 60 kDa and 30 kDa - 70 kDa and 30 kDa What are the molecular weights of the protein Y polypeptides? (pick 1 only) - 60 kDa, 50 kDa, and 30 kDa - 50 kDa each - 60 kDa and 30 kDa
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Question 9. // Help solve the picture and the questions that were cut off from the picture attached.
What are the molecular weights of the protein X polypeptides? (pick 1 only)
- 50 kDa each
- 60 kDa and 30 kDa
- 70 kDa and 30 kDa
What are the molecular weights of the protein Y polypeptides? (pick 1 only)
- 60 kDa, 50 kDa, and 30 kDa
- 50 kDa each
- 60 kDa and 30 kDa
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- The given protein, Protein X, is a heterotrimer - meaning it is a multimeric protein consisting of different polypeptide chains. Its molecular weight is 200 kDa. Using SDS-PAGE, the protein was characterized and the following profile is the result (attached in the picture). 1: Standard Protein Ladder 2: Protein X solution 3: Protein X solution + β-mercaptoethanol Determine the molecular weights of the three subunits of protein X based on the gel profile. Write the MW of each subunit and explain the obtained answer.In the protein denaturation experiment, which of the following can be a consequence of the air bubbles in the viscometry run for an aqueous solution of protein with a denaturant?a. Increased t0b. Decreased t0c. Increased nspd. Decreased nspAll of the statements about protein denaturation are true EXCEPT:a. The viscosity of linear proteins is greater than that of the globular proteins.b. Only the BME can disrupt a covalent bond while the other denaturants can just disrupt non-covalent bonds.c. Protein renaturation is possible but in some cases protein denaturation proceeds to protein degradation. d. Protein denaturation generally disrupts tertiary or quaternary structures onlyWhich of the following statements best describe(s) the mechanism by which correct protein folding takes place once the misfolded protein binds the open ring of groEL? Select all that apply. The groEL ring closes to isolate the protein and provide enough time for the protein to properly fold on its own. b and d The groEL ring closes to provide a hydrophilic space to isolate the protein and inhibit its aggregation with others until properly folded. The groEL ring closes to isolate the protein and provide steric hindrance that mechanically refolds the protein. The groEL ring closes to isolate the protein and decode the information necessary to achieve the correct three-dimensional structure. None of the above I picked "The groEL ring closes to provide a hydrophilic space..." but it was incorrect..
- Which of the following statements are true? Electrostatic interactions are the dominant forces in protein molecular recognition. When two proteins form a complex there is an unfavorable loss of rotational-translational entropy. Protein-protein interfaces are most often dry. The exclusion of water results in an unfavorable loss in rotational-translational entropy. The free energy change associated with the formation of an enzyme-substrate complex almost always results in an unfavorable reduction in conformational entropy of the proteins. Burial of an uncompensated positive charge inside proteins is usually unfavorable. So-called van der Waals’ interactions are essentially electrostatic in origin. Steric complementarity of the two partners forming a complex is essential to achieve optimal free energy of binding. Structural models of proteins obtained from low temperature crystallography are excellent descriptions of all biochemically relevant aspects of their function.Protein A will fold into its native state only when protein B is also present in the solution. However, protein B can fold itself into native confirmation without the presence of protein A. Which of the following is true? a. Protein B serves as precursor for protein A b. Protein B serves as molecular chaperone for protein A c. Protein B serves as ligand for protein A d. Protein B serves as structural motif for protein AOn an SDS-gel, If the distance traveled by the bromophenol blue dye is 7 cm, and the distance traveled by the protein band is 2.1 cm, the mobility of the protein is 0.3 30 3 30%
- You analyze a protein of 100 kDa using SDS-PAGE in the absence and presence of �-mercaptoethanol (BME) and observe the following band pattern in the gels: Which of the following statements about the protein is correct? (the image is attached) a. The protein consists of three polypeptide chains, two of which are connected via S-S bridges. b. The protein consists of two different polypeptide chains connected via S-S bridges. c. The protein has two different folding conformations. d. The protein consists of two different polypeptide chains linked to each other via non-covalent interactions.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?A gel filtration column with a fractionation range of 1.5-20 kDa is used to separate out the proteins shown below. If these proteins are collected into separate fractions in between the void volume and total volume, in which order will they elute? Indicate if any of the proteins are found in the void volume or total volume fractions. Protein Z - 3330Da Protein Y - 13kDa Protein X - 1.3kDa I. Total volume fraction II. Third protein fraction III. Second protein fraction IV. First protein fraction V. Void volume fraction
- Which of the following explains why beta sheets are the secondary structures observed in aggregates? a. Beta sheet structures can form between differing peptide chains allowing for aggregates b. This is a false statement; aggregates prefer fibrous structures like tropocollagen c. Beta sheet structures are formed with lots of charged residues that form ionic interactions to further stabilize the structure of the aggregate d. Beta sheet structures contain numerous cysteinyl residues that allow for formation of disulfide bonds for stabilizing the aggregateAn intermediate folding stage seen in protein denaturation or renaturation is called : a) domain b) motif c) subunit d) molten globule Proteins which do not renature spontaneously when denaturation conditions are removed may need the assistance of: a) a prosthetic group b) a higher salt concentration c) a lower temperature d) a chaperone protein The information needed for correct protein folding is encoded in: a) the surrounding molecules b) the protein’s amino acid sequence c) the pH of the aqueous medium d) the electrolyte composition of the aqueous solutionIn order to prepare a standard curve, you will do serial dilutions of the standard protein. Assume the protein concentration in tube A is 3 mg/ml and you take 0.5ml and add it to the next tube (tube B) containing 0.5ml of buffer. What is the concentration in tube B?