Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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- The diagrams below show the results of three FRAP experiments. Match the proteins to the statements. Protein B 1.0 0.8- 0.6- EVL 0.4- 0.2- 50 100 150 time (seconds) 0.2- 50 Protein A 100 150 time (seconds) 200 250 Protein that is completely tethered/anchored and does not move in the memebrane Protein that has some of it moving slowly while others are tethered/anchored in the membrane Protein that is fully mobile in the membrane Represent proteins associated with the cell membrane Represent cytoplasmic proteins that are moving around [Choose ] [Choose ] A, B and C None of these A Both A and B B с [Choose ] [Choose ] [Choose ] 200 250 50 Protein C 100 150 time (seconds) T 200 250arrow_forwardSo for this biology assignment I have a standard assay data for protein. A stock solution of BSA at 160mg/ml was made. Tubes were set to shown. Okay so Water (mL) has 1 in 1 chart 2 has 0.8 in chart 3 has 0.6 in chart 4 has 0.4 in chart 5 has 0.2 and in chart 6 has 0 BSA in chart 1 it’s 0 in chart 2 it’s 0.2 in chart 3 it’s 0.4 in chart 4 it’s 0.6 in chart 5 it’s 0.8 in chart 6 it’s 1.0 Reagent (mL) in chart 1 it’s a 3 in chart 3 it’s a 3 in chart 3 it’s 3 in chart 4 is 3 in chart 5 its 3 and chart 6 its 3 Then I have to figure out for each chart the amount of solute (mg) what it is in chart 1,2,3,4,5,6 same goes for volume of solution (mL) and Concentration of BSA (mL) And then the absorbance is 0 in chart 1, 0.072 in chart 2, 0.157 in chart 3, 0.302 in chart 4 and then for chart 5 its 0.457 and then in chart 6 its 0.621 I have then do the calculations and draw a standard curve in my graph sheet and explain what is the concentration of the unknown protein solution that…arrow_forwardIn Kjeldahl method, why the protein factors for some other cereal grains (e.g, wheat, oats) differ from that for corn?arrow_forward
- SDS is required to unfold proteins during SDS-PAGE electrophoresis and it is included in both the loading and running buffer. If SDS is not included in the running buffer.... the proteins in your sample may partially renature thus affecting migration. the gel will not conduct current in the absence of SDS. there is no effect on the samples. the proteins in your sample will be graded.arrow_forwardAmong the techniques below, which method is used to study protein-protein interaction in vivo? Group of answer choices co-IP TAP Y2H All of the abovearrow_forwardIn Western Blots and ELISAS, the following molecules are used: Tween-20 SDS Goat anti-rabbit IgG (whole molecule) – HRP Rabbit anti-egg albumin Bovine IgG Rabbit anti-bovine IgG – HRP Egg albumin (globular protein – what is Molecular weight?) Milk protein (globular protein – what is Molecular weight?) TMB Beta-mercaptoethanol Methanol HCl May you explain the reasons why they are used?arrow_forward
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