QUESTION 2For the peptide: TREATS, what would be they3ion?EATSTRETSATSQUESTION 3In the presence of 0.000005 M competitive inhibitor, an enzyme exhibits an apparent Km of 0.002M. If the Kq of theinhibitor is 0.0000003 M, what is the true Km of the enzyme? Give your answer with 3 significant figures anscientific notation. For example, 0.000023434 is 2.34eQUESTION 4Approximately how many domains are in an 82.5 kDa protein?O a.270 Mostly cloudyAClick Save and Submit to save and submit. Click Save All Answers to save all answers.Tune here to search

We are authorized to answer one question at a time since you have not mentioned which question you…

Answered: For the peptide: TREATS, what would be…

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

QUESTION 6 What is the three ketter code for each peptide(a) KFYV(b) ERSC(c) PIMFThe 3-letter code for Peptide (a) is: The 3-letter code for Peptide (b) is: The 3-letter code for Peptide (c) is:
QUESTION 22 When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Allosteric activation Zymogen activation Covalent modification Competitive inhibition Allosteric inhibition
Question 1Predicting Secondary Structure Which of the following peptides is more likely to take up an -helical structure, and why? (a) LKAENDEAARAMSEA (b) CRAGGFPWDQPGTSN
If an enzyme catalyzed reaction has a KM of 5mM and a Vmax of 60 nm/sec, the substrate concentration at 30 nM/sec is? Thank you.
If the data from an enzyme experiment is plotted as a Lineweaver-Burk plot, and the Vmax is 0.02 mol/sec, and x-intercept is –2.5 mM then what is the KM value? Show yourwork/reasoning.
Question 11. // Hint: Isoelectric focusing separates proteins based on their pI values, and can separate proteins that only differ by a net charge of ±1.±1. Recall that an amino acid residue with a negatively charged R group has a relatively low isoelectric point (pI) where it has zero net charge. Likewise, an amino acid residue with a positively charged R group has a relatively high isoelectric point (pI) where it has zero net charge. Order from Low pH to High pH
Question 9 Imagine you have a mixture of 2 proteins. Protein A is 3x the mass of protein B. Both have net negative charges, but protein B has 3x more negative charges than protein A. If you load the mixture onto an electrophoresis gel and apply an electric field, which will move faster/slower through the gel? Explain your reasoning.
Question 6 Below is a BSA standard curve and the duplicate values of absorbance for 3 samples. Calculate the concentration of BSA in each sample and say if the standard curve is adequate for each of these samples? Why or why not? If not, what would you do to fix this? Show your calculations.
QUESTION 2An isocitrate dehydrogenase assay was performed on the enzyme sample and found to give an absorbance change at 340nm of 0.5 absorbance units perminute. Given that the molar absorption coefficient (E) is 6220 M-1 cm-1 and the pathlength is 1cm, what is the rate of the enzyme catalysed reaction in umol perminute per mL?
Calculate your dilution strategyto make a 625 ng/mLHRP solution from a 12.5 μg/mL stock given the totalvolume of enzyme youwillneed for your condition this week. Note if you are testing pH, you only need to calculate one enzyme dilution because all other pHs will use the same strategy.
Answer TRUE or FALSE.a. According to the lock-and-key model of enzyme action, the active site of an enzyme is not flexible in shape.b. In an enzyme-catalyzed reaction, the compound that does not undergo a chemical change is called the substrate.c. The nonprotein portion of a conjugated enzyme is not the enzyme’s active sited. Simple enzymes are composed only of protein; conjugated enzymes have nonprotein cofactors.
Question: A. To explore the consequences of coupling ATP hydrolysis under physiological conditions to a thermodynamically unfavorable biochemical reaction, consider the hypothetical transformation X⟶Y, for which Δ?′°=20.0 kJ/mol. What is the ratio of [Y]/[X][Y]/[X] at equilibrium? B. Suppose XX and YY participate in a sequence of reactions during which ATP is hydrolyzed to ADP and Pi. The overall reaction is X+ATP+H2O⟶Y+ADP+Pi Calculate [Y]/[X] for this reaction at equilibrium. Assume that the temperature is 25.0 °C and the equilibrium concentrations of ATP, ADP, and Pi are 1.00 M each. C. We know that [ATP], [ADP], and [Pi] are not 1.00 M under physiological conditions. Calculate [Y]/[X] for the ATP‑coupled reaction when the values of [ATP], [ADP], and [Pi] are those found in rat myocytes. Metabolite Concentration in rat myocytes (M) ATP 8.05x10-3 ADP 0.93x10-3 Pi 8.05x10-3

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

For the peptide: TREATS, what would be the y3 ion? EATS TRE TS ATS