F2Question 4: Tropomyosin is a 93 kDa protein which sediments at 2.6S (the sedimentation coefficient Sis a linear measure of the rate of sedimentation during centrifugation). Hemogloblin is a smallerprotein (63 kDa), but it sediments faster at 4.3S. The two proteins are drawn to scale in the figurebelow. Using this information, explain why the larger protein (tropomyosin) sediments more slowlythan the smaller protein (hemogloblin). How would this change if you treated both proteins with SDSand B-mercaptoethanol prior to sedimentation via centrifugation?#3ED80F3C$4RF888V%5hemoglobinF5TG^6BMacBook AirF6YSOUPRH&7NAdF7UtropomyosinJ* 008DIIFBM-(9KDDF9O<)OLAF10P♡

Hemoglobin - is a oxygen and carbon dioxide transport protein kin red blood cells. It is a spherical…

Answered: Question 4: Tropomyosin is a 93 kDa…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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How many copies of a protein need to be presentin a cell in order for it to be visible as a band on an SDSgel? Assume that you can load 100 μg of cell extract ontoa gel and that you can detect 10 ng in a single band by sil-ver staining the gel. The concentration of protein in cellsis about 200 mg/mL, and a typical mammalian cell has avolume of about 1000 μm3 and a typical bacterium a vol-ume of about 1 μm3. Given these parameters, calculatethe number of copies of a 120-kd protein that would needto be present in a mammalian cell and in a bacterium inorder to give a detectable band on a gel. You might try anorder-of-magnitude guess before you make the calcula-tions.
shift tab fn 2 3 4 caps lock Questions: For the first two questions, refer to this photo of a SDS PAGE of ladder and antibody. The lane on the left (1) shows a protein ladder and the lane on the right (2) shows antibody. 5 esc Question la. How many different proteins are in the protein ladder? 1b. Ladder and antibody samples are loaded into different the gel. 1c. The approximate size (in kDa) of "Heavy Chain" is: 1d. The approximate size (in kDa) of "Light Chain" is: ! 1 ܝ A @ 2 N A W # 3 S E A $ 4 D B R % 5 X V с I F on An T 9 ty Chre 49 K 25 Kc MacBook P 6 V
Please explain!!! select all that are right the same Protein X was purified from tissue source A and tissue source B, yielding the following results: Protein X, sample A: specific activity = 100 U/mg; fold-purification = 200 Protein X, sample B: specific activity = 1000 U/mg; fold-purification = 100 Which of the following statements are correct? a) Protein X, sample A has a higher level of purity than Protein X, sample B. b) Protein X, sample B has a higher level of purity than Protein X, sample A. c) Tissue source A has a higher specific activity for Protein X than tissue source B. d) Tissue source B has a higher specific activity for Protein X than tissue source A.
Clathrin coat features and activities it participated include Its protein chains, triskelion, are arranged with the membrane through adaptors to form invaginations or pits. Its protein chains, triskelion, are arranged with the membrane through adaptors to form invaginations or pits. Its protein chains, triskelion, are arranged with the membrane through adaptors to form invaginations or pits. Its protein chains, triskelion, are arranged with the membrane through adaptors to form invaginations or pits.
How many copies of a protein need to be present in a cell in order for it to be visible as a band on an SDS gel? Assume that you can load 100 µg of cell extract onto a gel and that you can detect 10 ng in a single band by sil ver staining the gel. The concentration of protein in cells is about 200 mg/mL, and a typical mammalian cell has a volume of about 1000 μm³ and a typical bacterium a vol ume of about 1 µm³. Given these parameters, calculate the number of copies of a 120-kd protein that would need to be present in a mammalian cell and in a bacterium in order to give a detectable band on a gel. You might try an order-of-magnitude guess before you make the calcula tions.
estion 2 Using the Chou-Fasman rules (without calculating numerical probability) predict the secondary structural elements in the following protein sequence. Give the residue numbers or residue range and state the secondary structure. Arg- Pro-Glu- Lys-Val-Thr-Trp-Tyr-Phe-lle Arg-Arg-Asn-Pro-Gly-Asp-Arg 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16. 17 For the toolbar, press ALT+F10 (PO) or ALT+RN+F10 (Mac)
1CFD CALCIUM-FREE CALMODULIN How long is the protein’s primary sequence?Does this protein have any secondary, tertiary and/or quaternary structures present?Are there any molecular additions to this protein that are not amino ac
UESTION 8 For a student's fourth year honours project, a protein with molecular weight 75,000 is the target. The student needs to perform dialysis on this protein to eliminate the present ammonium sulfate. If the molecular weight cut off of the dialysis tubing is 100,000, what will happen? Some of the protein will stay in the dialysis bag; some will exit the dialysis tubing bag. The protein will be retained in the dialysis tubing bag. The protein will exit the dialysis tubing bag. O O O
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