In what order would the proteins elute from a size exclusion column (limit 50- 40,000)? Protein...
In what order would the proteins elute from a size exclusion column (limit 50- 40,000)? Protein Molecular weight 1- 90 KDa 2- 27,000 KDa 3- 300 KDa
Homework Answers
The 90kDa protein will elute first because of its very small size when compared to the pore size. The 300kDa protein will elute second followed by the 27000kDa protein as the size of the pores in the column is specific to this protein size.
Add Answer to:
In what order would the proteins elute from a size exclusion
column (limit 50- 40,000)? Protein...
Which of these 5 proteins will elute first from the gel filtration (size exclusion) column? Serum albumin (68 kDa) a-la...
Which of these 5 proteins will elute first from the gel filtration (size exclusion) column? Serum albumin (68 kDa) a-lactalbumin (14.2 kDa) O Lactoferrin (87 kDa) k-casein (19 kDa) O b-lactoglobulin (18 kDa) O Glucagon activation of a G protein-coupled membrane receptor (GPCR) induces GTP binding to which of the following membrane anchored proleins? Gbg Phospdlipase A2 None of the mentioned options The GPCR itself Ga Which of the following sphingolipids is a phospholipid? Sphingomyelin Gangliosides None of the mentioned...
what is the principle of gel filtration chromatography? 19 E 3 2 1 AaBbceDdEe ABCDdee AaBbCcDc...
what is the principle of gel filtration chromatography?
19 E 3 2 1 AaBbceDdEe ABCDdee AaBbCcDc AaBbCcDdE No Spacing Heading 1 Heading 2 7. A. What is the principle of Gel filtration chromatography? (1 point) B. In gel filtration chromatography, what is the stationary phase and the mobile phase (that we used in our lab experiment)? (1 point) C. In what order would the proteins elute from a size exclusion column (limit 50- 40,000) (1 point) Protein Molecular weight KDa...
NOTES: To separate on a size-exclusion column, differences in MW need to be greater than 10%....
NOTES: To separate on a size-exclusion column, differences in MW need to be greater than 10%. To separate proteins by charge, the difference in pI must be at least 0.5 pH unit. Consider the table of four proteins below: Protein Size pI Size exclusion Charge at pH 7.4 DEAE-elution 1 49 kDa 6.8 2 51 kDa 8.1 3 53 kDa 6.4 4 99 kDa 8.3 5 106 kDa 3.8 6 143 kDa 7.9 (a) In what order would the proteins...
In what order will the following proteins elute from a Sephadex G-150 column: catalase (222 kDa),...
In what order will the following proteins elute from a Sephadex G-150 column: catalase (222 kDa), chymotrypsin (21.6 kDa), concanavalin B (42.5 kDa), lipase (6.7 kDa), and lysyl oxidase (30 kDa)?
Question 8 7--22- The following proteins were eluted from a G100 size exclusion column (exclusion limit:100,0000...
Question 8 7--22- The following proteins were eluted from a G100 size exclusion column (exclusion limit:100,0000 of protein molecules fractionated from G 100 size exclusion column. The elution curve revealed 5 peaks (below), identify the molecule/s eluted as peak number 2. Myoglobin, MW:68,500, Myosin, MW:524,000, Immunoglobulin M:MW375,000, serum albumin. MW: 68,500, Cytochrome c,MW: 13,370, Polypeptide A: MW: 10,000 and Chymotrypsinogen, MW: 23,240 Question 9
a. Which spot corresponds to the protein with the largest molecular weight? b. When pH = 7, what order would the follow...
a. Which spot corresponds to the protein with the largest
molecular weight?
b. When pH = 7, what order would the following peptides elute
from a column filled with cation exchange resin? Size exclusion
column?
Protein 1 – 400 kDa;
10%A 5%E, 5%F, 10% G, 5% H, 10%I, 10%K, 10%L 10%R, 5%P, 5%S, 10%W,
5%Y
Protein 2: 40 kDa
5%A, 5%C, 5%D, 5%E, 5%F, 10%G, 5%I, 10%K, 5%L, 5%M, 5%N, 10%P, 5%R,
5%S, 5%T, 5%V, 5%W,
Protein 3 – 175...
You have a mixture of the proteins listed below. Protein pI Molecular Weight (kDa) A 3.1...
You have a mixture of the proteins listed below. Protein pI Molecular Weight (kDa) A 3.1 265 B 6.9 93 C 10.3 96 D 7.1 43 E 8.6 189 1. You load the protein mix onto a cation exchange column at pH 5. Next, you apply a "washing" step by passing through buffer at pH 5. Finally, for your elution step, you apply a pH gradient starting from pH 2.0 to pH 13.0. (A gradient buffer system allows you to...
9. In the mixture of proteins you have protein A: 35 kDa, protein B: 15 kDa,...
9. In the mixture of proteins you have protein A: 35 kDa, protein B: 15 kDa, protein C: 58 kDa, protein D: 150 kDa. Propose the chromatographical method to separate them. Write in which order they would elute from the column. 10. What is the best chromatographical method to separate fluorescein and amide black? They are organic dyes.
How do you elute proteins from an affinity column where the protein is bound to a...
How do you elute proteins from an affinity column where the protein is bound to a ligand which is attached to beads? Add a large amount of the free ligand that specficially binds the protein to compete for binding to the protein. Add SDS to denature the proteins. Add increasing amounts of salt to compete for ionic bonds with the protein. Wash the column with a large amount of buffer so that even the smallest molecules can filter through.
9. The following proteins were identified in a mixture. protein te precipitate MW (kDa) 4.8 22...
9. The following proteins were identified in a mixture. protein te precipitate MW (kDa) 4.8 22 IMRSO) 45% 80% 65% 20% 30% 45% 5.3 6.8 9.50 un 115 5.3 th(cont.) a) What is meant by "salting out" a protein using MgSO.? What happens on a molecular level? b) Draw a gel indicating proteins 1-6 order of elution in SDS-PAGE. Label where sample would start so I am clear on the validity of your answer. c) Draw their order of elution...
Which of these 5 proteins will elute first from the gel filtration (size exclusion) column? Serum albumin (68 kDa) a-lactalbumin (14.2 kDa) O Lactoferrin (87 kDa) k-casein (19 kDa) O b-lactoglobulin (18 kDa) O Glucagon activation of a G protein-coupled membrane receptor (GPCR) induces GTP binding to which of the following membrane anchored proleins? Gbg Phospdlipase A2 None of the mentioned options The GPCR itself Ga Which of the following sphingolipids is a phospholipid? Sphingomyelin Gangliosides None of the mentioned...
what is the principle of gel filtration chromatography?
19 E 3 2 1 AaBbceDdEe ABCDdee AaBbCcDc AaBbCcDdE No Spacing Heading 1 Heading 2 7. A. What is the principle of Gel filtration chromatography? (1 point) B. In gel filtration chromatography, what is the stationary phase and the mobile phase (that we used in our lab experiment)? (1 point) C. In what order would the proteins elute from a size exclusion column (limit 50- 40,000) (1 point) Protein Molecular weight KDa...
Question 8 7--22- The following proteins were eluted from a G100 size exclusion column (exclusion limit:100,0000 of protein molecules fractionated from G 100 size exclusion column. The elution curve revealed 5 peaks (below), identify the molecule/s eluted as peak number 2. Myoglobin, MW:68,500, Myosin, MW:524,000, Immunoglobulin M:MW375,000, serum albumin. MW: 68,500, Cytochrome c,MW: 13,370, Polypeptide A: MW: 10,000 and Chymotrypsinogen, MW: 23,240 Question 9
a. Which spot corresponds to the protein with the largest
molecular weight?
b. When pH = 7, what order would the following peptides elute
from a column filled with cation exchange resin? Size exclusion
column?
Protein 1 – 400 kDa;
10%A 5%E, 5%F, 10% G, 5% H, 10%I, 10%K, 10%L 10%R, 5%P, 5%S, 10%W,
5%Y
Protein 2: 40 kDa
5%A, 5%C, 5%D, 5%E, 5%F, 10%G, 5%I, 10%K, 5%L, 5%M, 5%N, 10%P, 5%R,
5%S, 5%T, 5%V, 5%W,
Protein 3 – 175...
9. In the mixture of proteins you have protein A: 35 kDa, protein B: 15 kDa, protein C: 58 kDa, protein D: 150 kDa. Propose the chromatographical method to separate them. Write in which order they would elute from the column. 10. What is the best chromatographical method to separate fluorescein and amide black? They are organic dyes.
How do you elute proteins from an affinity column where the protein is bound to a ligand which is attached to beads? Add a large amount of the free ligand that specficially binds the protein to compete for binding to the protein. Add SDS to denature the proteins. Add increasing amounts of salt to compete for ionic bonds with the protein. Wash the column with a large amount of buffer so that even the smallest molecules can filter through.
9. The following proteins were identified in a mixture. protein te precipitate MW (kDa) 4.8 22 IMRSO) 45% 80% 65% 20% 30% 45% 5.3 6.8 9.50 un 115 5.3 th(cont.) a) What is meant by "salting out" a protein using MgSO.? What happens on a molecular level? b) Draw a gel indicating proteins 1-6 order of elution in SDS-PAGE. Label where sample would start so I am clear on the validity of your answer. c) Draw their order of elution...
Most questions answered within 3 hours.
-
A sock stuck to the side of a clothes-dryer barrel has a
centripetal acceleration of 24...
asked 22 minutes ago -
A perfect gas undergoes an isentropic process such that its
volume doubles. If the ratio of...
asked 42 minutes ago -
list the elements in groups 3A to 6A in the same order as in the
periodic...
asked 51 minutes ago -
Estimating effect size. Peng and Chen (2014)
evaluated effect size estimates for various tests. In their...
asked 1 hour ago -
Write a script in MySQL that creates and calls a stored
procedure name test. This procedure...
asked 1 hour ago -
If we test the following: H0: μ = 17
vs. H1: μ ≠ 17 and the...
asked 1 hour ago -
in the past year TVG had revenues of 3 million, cost
of goods sold of $25...
asked 1 hour ago -
4) In a polypeptide, which bond cannot rotate because of its
partial double bond character?
The...
asked 1 hour ago -
Assume that in the short run L = 1,000 and K = 100. 1. What is...
asked 1 hour ago -
At a given temperature, 2.06 atm of H2 and 3.7 atm of Br2 are
mixed and...
asked 1 hour ago -
Sodium reacts with Hydrochloric acid to form sodium chloride and
hydrogen gas. 2Na(s)+ 2 HCl(aq)-> 2...
asked 1 hour ago -
The following circuits (1 & 2) are combined to form a
series-parallel circuit and resulting circuit...
asked 1 hour ago