answer:1) pI,pH(I),IEP all are nomenclature to represent the isoelectronic point of a molecule where it carries no net charge below it, it will carry a negative charge and above it, it will carry a positive charge
so A is an incorrect statement because it carries a positive charge at pH>7
2) E is the correct means all the above are collect
In electrophoresis charged molecules are transported through a solvent by an electrical field. And for protein separation, it depends on the all the given factors A, B, C, D
3)D is the correct option because a peptide bond is a like amide bond (R-CO-NH-R), formed by condensation type of reaction in which NH2 and -COOH group of two amino acid combine and form peptide bond and H2O as side product
A protein has a pl 4.5, which of the following is incorrect about the protein the...
32. Which of the following would make a protein of a large size move faster through an SDS gel electrophoresis separation? a. add more protein to your sample b. add more buffer c. remove some buffer d. decrease the acrylamide concentration of the gel e. increase the acrylamide concentration of the gel 33. Which of the following statements are accurate? i. SDS binds to proteins, introducing a negative charge which is proportional to the length of the protein primary structure....
ANSWER ALL 1) Which of the following is the stationary phase in size exclusion chromatography? A. resin B. mixture of proteins C. solvent or buffer D. none of these 2) Suppose you wish to purify a protein that has many positively charged residues from a mixture of proteins. Which of the following columns would elute the protein the fastest? A. column packed with neutral resin B. column packed with positively charged resin C. column packed with negatively charged resin D....
Protein molecules in solution can be separated from each other by taking advantage of their net charges. In the electric field between two electrodes, a positively charged particle moves toward the negative electrode and a negatively charged particle moves toward the positive electrode. This movement, known as electrophoresis, varies with the strength of the electric field, the charge of the particle, the size and shape of the particle, and the buffer/polymer gel combination through which the protein is moving. The...
Please EXPLAIN your answer If protein A has a pl of 3.1, protein B has a pl of 6.8, and protein C has a pl of 8.9, which protein would elute FIRST from a cation exchange column at pH 7? н H R-C-COOH Z R R -C-C00“ -C-000 +NH + NH3 NH2 Net charge: +1 Cationic form Zwitterion (pl) Anionic form protein C pl = 8.9 pH <pl cationic protein B pl = 6.8 pH = pl neutral protein A...
Protein A has an isoelectric ph of 3. Protein B has an isoelectric ph of 5. Protein C has an isoelectric ph pf 7. Given these proteins, predict the direct of movement in the electrophoresis chamber is the buffer in the chamber has a ph of 6. Explain your reasoning.
(iln 2. Use the letters given to answer the questions below for full credit Protein name pl A Nonheme iron-containing fermitin (Pf) B Pynuvate: ferredoxin oxidoreductase, alpha Subunit (PorA) 44613 CGTP-binding proteia (Gtpl) D Co-chaperone (GiroES) E Adhesin-thiol peroxidase (TagD) FI Fumarase (Fund) 19,155 5.49 5.81 40,444 5.53 12,860 6.59 18,161 8.18 50,844 7.29 i) (5 points) Sketch the Isoelectric focusing gel after the separation of above proteins is performed. Clearly label everything needed for full credit. i) (5 points)...
Biochem help 2 14. What would be the net charge on the dipeptide Ser-His at pH- 6.04? (Choose the one best answer.) a) 1.5 b) +1; c) +0.5 d) 0 e) -0.5; 15. The pKa of a lysine side chain in a protein ending up on the outside of a globular protein has a different pKa than if the lysine is buried within the interior of a protein. What would be the expected pKa of a side chain of lysine...
6. You are given a mixture of proteins that you analyze by standard 2-D electrophoresis, with the following results for isoelectric points and apparent molecular weights: protein A (Mr 110,400; pl 4.60), protein B (Mr 10,100; pl 6.93), protein C (Mr 65,200; pI 7.84), and protein D (M 25,000; pI 8.15) a. After the 2-D separation, which protein will be in the upper left quadrant of the gel. given that e cathode-proximal end of the isoelectric focusing gel was on...
wollo 5. Given amino acids LG, and possibly made is the maximum kinds of tetrapeptides could be B. C. D. E. 12 16 9 81 6. "SDS' applied in electrophoresis can B dye the protein make protein negatively charged denature the protein form covalent bond with protein B and C D E. 7. Which of the following is the conjugate base of Hoho NH OH но тон, но NH он но NH, yo
1. Which is a correct description of the use of separation techniques to separate a dipeptide from a pentapeptide? a. the dipeptide emerges faster than the pentapeptide from a gel filtration column b. the dipeptide migrates faster towards the cathode than the pentapeptide on SDS-PAGE c. the dipeptide migrates to a more anodal position than the pentapeptide on electrofocusing d. the dipeptide sediments faster than the pentapeptide in an ultracentrifugal field e. none of these methods would separate the dipeptide...