(a) 1Normalized fluorescence0.80.60.40.205055OM0.100 M0.200 M0.300 M0.500 M1.00 M2.00 M6011358865Temp. (°C)707580Where is fully folded protein?• Where is fully unfolded protein?• Where is partially folded protein?• To what does SYPRO orange bind?• Why does fluorescence increase as a function oftemperature?● Define a melting temperature for a protein.• Demonstrate how an estimated meltingtemperature of the protein in zero molar ligandcan be determined.• What is the effect of increasing the molarconcentration on melting temperature for thisprotein?• Why is melting temperature a useful measurementto make for a protein especially if youare interested in protein aggregation?

There are four classes of biological macromolecules - proteins, nucleic acid, lipids and…

Answered: (a) 1 Normalized fluorescence 0.8 0.6…

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

See similar textbooks

Similar questions

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.
Given the description of four different proteins above: Which protein will have the highest mobility in an SDS-PAGE gel?
What is the function of sodium dodecyl sulfate (SDS) in SDS-PAGE? stabilizes the gel matrix, improving resolution during electrophoresis SDS solubilizes proteins to give them uniformly negative charges, so the separation is based purely on size. SDS raises the pH of the gel, separating multiunit proteins into individual subunits. SDS solubilizes proteins to give them uniformly positive charges, so separation is based purely on pH.
B W S sult, it makes the protein Why is denaturing the proteins necessary for SDS PAGE to work? Use YOUR OWN X mand 3 E D с $ R F 5 Lê 6 T G MacBook Pro B Y H U N J 8 I M 9 K O I O L 44 P command . : 8 ; x { + C option ? I } 1 M
Consider the following properties of the protein components of a sample mixture as provided in the table below. Protein Molecular IpH Percentage of polar amino acid residues Weight (kDa) (%) АСЕ 200 7 20 CLU 25 65 DIA 100 10 40 НЕА 50 80
(a) 0.25 Turbidity (AU) 0.20- 0.15- 0.10- 0.05- 0.00+ 0 Wt Mutant 1 Mutant 2 Mutant 3 Mutant 4 2 8 Incubation time (h) 6 10 Define turbidity. • How is turbidity related to protein aggregation? • Where is protein with no aggregation for any condition? • Where is protein with maximal aggregation for any condition? • What area of the plot tells you about the rate of aggregation for any condition? 12 • What area of the plot tells you about total aggregation for any condition? • Slow, medium, and fast rates of aggregation are shown - which samples fall into each category? ● Two amounts of total aggregation are shown - which samples fall into each category? • Name two samples that have the similar rates of aggregation, but different amounts of total aggregation. • Name two samples that have different rates of aggregation, but similar amount of total aggregation. ● Why is protein turbidity a useful experiment to perform for a protein especially if you are interested in protein aggregation?
7. 1 B e here to search Required Study the two diagrams below. Diagram A 2 1 Diagram B 2 Based on the sequence of steps (1, 2, 3), which of the diagrams shows what would happen to proteins made at the ribosomes and transported to the outside of the cell? Diagram A Diagram B Both Diagram A and Diagram B Neither Diagram A nor Diagram B DELL 40)
(A) What property of a protein might make it difficult to transfer it from polyacrylamide gel to nitrocellulose? Explain your reasoning. (B) What parameter of the gel transfer protocol can be adjusted that might help improve the transfer of these problematic proteins to the nitrocellulose membrane? Explain your reasoning. (C) How can we check if proteins have been successfully transferred from the polyacrylamide gel to nitrocellulose?
On an SDS-gel, If the distance traveled by the bromophenol blue dye is 7 cm, and the distance traveled by the protein band is 2.8 cm, the mobility of the protein is 40 4 40% 0.4
Which one of the amino acids below would most likely be present in the part of the protein touching the membrane's hydrophobic tails? Choice 1 of 5:lysineChoice 2 of 5:tryptophanChoice 3 of 5:threonineChoice 4 of 5:glutamineChoice 5 of 5:aspartic acid Q2 sugar Grading comment: Where do plants make sugar? Choice 1 of 4:photosystem II of the light reactionsChoice 2 of 4:glycolysisChoice 3 of 4:the Calvin cycleChoice 4 of 4:photosystem I of the light reactions Q3 willow experiment Grading comment: The Willow Experiment shows that: Choice 1 of 4:the seeds that got only water did not do photosynthesisChoice 2 of 4:oxygens in heavy water emerge as heavy oxygen gasChoice 3 of 4:the mass of a tree is derived by absorption of sunlight energyChoice 4 of 4:the mass of a tree does not derive from its soil Q4 cells Grading comment: If a cell is placed into an extremely salty solution, the cell will: Choice 1 of 3:swellChoice 2 of 3:shrinkChoice 3 of 3:no change…
You have purified Protein 'X' and you want to know its concentration. As we learned, you can calculate concentrations by simply measuring UV280 absorbance of protein solutions. Using a UV spectrophotometer, you measured an absorbance of 0.6. Given that Protein X has an absorptivity (or extinction coefficient) of 0.2 mL•mg-cm at 280 nm, what is the concentration of purified protein solution (assume the light path is 1 cm)? -1 O A. 3 g/mL B. 3 mg/mL OC.0.2mg/mL OD.0.2 g/mL OE. 0.6 g/mL
What are the roles of sodium dodecyl sulfate (SDS) in two-dimensional electrophoresis? to cause bound proteins to have a large positive charge to denature proteins to cause bound proteins to have a large negative charge to preserve zero net charge of the proteins to preserve the structure of the bound proteins Incorrect

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS