Question

Your protein of interest will not form crystals, and it is 100 kDa in size. You...

Your protein of interest will not form crystals, and it is 100 kDa in size. You would still like to study it structurally. What technique will you explore next, and why? What limitations might you encounter?

0 0
Add a comment Improve this question Transcribed image text
Answer #1

The following image is of my notes and will guide you to techniques used for the analysis of structure of protein

9:48 PM 0.86K/s 4G 37% Titre Several methods are currently used to determine the structure of a protein, including X-ray crystallography, NMR spectroscopy, and electron microscopy. Each method has advantages and disadvantages. In each of these methods, the scientist uses many pieces of information to create the final atomic model. Primarily, the scientist has some kind of experimental data about the structure of the molecule. For X-ray crystallography, this is the X-ray diffraction pattern. For NMR spectroscopy, it is information on the local conformation and distance between atoms that are close to one another. In electron microscopy, it is an image of the overall shape of the molecule.

Add a comment
Know the answer?
Add Answer to:
Your protein of interest will not form crystals, and it is 100 kDa in size. You...
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Not the answer you're looking for? Ask your own homework help question. Our experts will answer your question WITHIN MINUTES for Free.
Similar Homework Help Questions
  • Q. Briefly in point form or using a flow chart, describe what chromatographic techniques you would...

    Q. Briefly in point form or using a flow chart, describe what chromatographic techniques you would use to completely separate a mixture of the 4 proteins listed below. After each part of the techniques, BRIELFY outline what that particular technique accomplished (or show it in your diagram). Protein A: 35 kDa, pI = 3.5 Protein B: 35 kDa, pI = 8.5 Protein C: 100 kDa, pI = 8.5 Protein D: 100 kDa, pI = 3.5

  • 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...

  • 6. If you have two proteins with unknown concentrations (4 points): -sample A: a protein that...

    6. If you have two proteins with unknown concentrations (4 points): -sample A: a protein that contains polar uncharged amino acids, negatively charged amino acids and arginines, size: 40 KDa -sample B: a protein rich in lysines, size: 100 KDa A. If you want to separate both proteins, which acrylamide gel concentration would you chose? B. Which staining method (s) would you chose for this gel? Why?

  • During recrystallization, you allow your product to form solid crystals slowly upon cooling. Why?

    During recrystallization, you allow your product to form solid crystals slowly upon cooling. Why?

  • You hypothesize that your protein of interest moves from the mitochondria to lysosomes when a cell...

    You hypothesize that your protein of interest moves from the mitochondria to lysosomes when a cell is exposed to the drug Fantasalin. A. Design a microscopy experiment to test this hypothesis. Please include the LABELS and type(s) of microscopy you would use. Also, please draw illustrations of what you predict your experiment to look like. B. Design an experiment to test this hypothesis using cell fractionation and SDS-PAGE. Please include what samples you would collect to run on the gel,...

  • 4.     (Challenge) You are purifying a protein from the brain of patients with an unusual type of...

    4.     (Challenge) You are purifying a protein from the brain of patients with an unusual type of dementia triggered by a coronavirus and you hypothesize that this protein may be a signature molecule of this type of dementia. To pursue this hypothesis, you collect brain tissue from patients post mortem, do differential centrifugation, density gradient centrifugation, CM (carboxymethyl cellulose) ion exchange chromatography and gel filtration. You then assess the purity of your protein using both native and SDS gel electrophoresis. The...

  • Question 6 You and your G-protein coupled receptors o You have encountered G-protein coupled receptors in...

    Question 6 You and your G-protein coupled receptors o You have encountered G-protein coupled receptors in Intro Bio I lecture (or soon will), and will encounter them briefly again in Intro Bio II. You will spend 2 or 3 lectures on them in Cell Bio. They are integral (transmembrane) proteins embedded in the plasma membrane of every eukaryotic cell in your body. We will treat them as being 50 Angstroms in diameter. Considering the plasma membrane scaled up to the...

  • 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...

  • Part B. Working as a Biology 499 student, your supervisor would like to examine the protein- protein interaction...

    Part B. Working as a Biology 499 student, your supervisor would like to examine the protein- protein interaction in the tyrosine kinase complex as shown in the following figure. Specifically, you are asked to show the direct interaction between Sos, Ras and GRB2, in the presence or absence of EGF. Sinding of CAB2 and Sou couples recrgeo to inacie Two separate dishes of cells were each transfected with a different type of Vector DNA: HA GST, HA-Sos. After growing for...

  • During a recrystallization procedure, if crystals do not form upon cooling to 0 °C: i) Without...

    During a recrystallization procedure, if crystals do not form upon cooling to 0 °C: i) Without changing the volume of the solution, what are three methods that can be used to induce nucleation (crystal growth)? Describe each method in one sentence (each). ii) If none of your methods of inducing nucleation works (which you described in Part i), then what experimental steps would you take next in order to achieve recrystallization of the compound? Offer details. Assume that you do...

ADVERTISEMENT
Free Homework Help App
Download From Google Play
Scan Your Homework
to Get Instant Free Answers
Need Online Homework Help?
Ask a Question
Get Answers For Free
Most questions answered within 3 hours.
ADVERTISEMENT
ADVERTISEMENT
ADVERTISEMENT