### Protein Structure and Oxygen Binding#### 9. In the α-helixA. **there are no hydrogen bonds**B. **the peptide chain is fully extended**C. **the peptide chain bends back on itself**D. **there are hydrogen bonds perpendicular to the helix axis**E. **None of the above**#### 10. The Bohr effect for oxygen binding states thatA. **myoglobin binds oxygen more tightly than Hb.**B. **hemoglobin will bind oxygen very tightly when the CO2 concentration is high.**C. **as the pH goes up, Hb binds oxygen less tightly.**D. **Hb's ability to bind oxygen increases with higher oxygen concentration.**E. **None of the above**

The four levels of protein structure organization are primary, secondary, tertiary and quaternary…

Answered: 9. In the a-helix A. there are no…

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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What is one reason that protein folding intermediates are prone to aggregation? a. Their hydrophobic chemical groups are exposed to solvent b. They have not formed enough hydrogen bonds c. They are not globular enough d. They have not formed any disulfide bonds
Give explanation of all four otherwise leave it
2. Come up with a synthesis strategy to make the dipeptide ser-asp. To do this you will need to provide a lot of information. a. Synthesis schemes starting from unmodified the amino acids, ser and asp, including:1. Initial protection of the amino acids2. Coupling of the amino acids using PyBop3. Deprotection of the N and C termini
9. Shown below is a binding pocket for a protein with a ligand bound. The ligand interacts with a serine and a valine side chain. ligand a. Briefly explain, in terms of Ka, the effect of a mutation that replaces the serine residue with a valine residue. b. Briefly explain, in terms of Kd, the effect of a mutation that alters the ligand (as seen below) binding to the original, unmutated, binding site. :0: ligand 2
I only need numbers 39-41
Indicate which of the following descriptions is true about the biochemical depicted here: NH₂ +41 5 HO- он он OH OH OH a. Ribonucleotide b. Complementary to dTTP c. Purine d. Key reagent in Sanger sequencing e. Answers b., c. and d. are correct
1. The CFTR protein is a chloride channel in the cell membrane. Use your understanding of the biochemical properties/categories of amino acids and how they interact with membrane phospholipids to predict the distribution of charged/polar, and non-polar amino acids within the domains of CFTR listed below. Consider one category to include the charged amino acids and the polar amino acids and the other category to include the non-polar amino acids. For each domain, predict which category of amino acids is likely to be most abundant. Also, explain the rationale behind your prediction. Protein domain Prediction (Charged/Polar or Non-Polar amino acids?) Explanation for prediction TMD1 and TMD2 (transmembrane domains, parts 1-12) ECLs and ICLs (extracellular and intracellular loops) NBD1 and NBD2 R
Identify the incorrect statement regarding the polypeptide, Myoglobin. Select one: a. The interaction between Myoglobin and O2 is homotopic in nature as indicated by a Hill coefficient n = : 1 b. Myoglobin is found predominantly in muscle tissue because it facilitates oxygen diffusion. c. The majority of Myoglobin's secondary structure is composed of alpha-helices d. Myoglobin has a higher affinity for oxygen than Hemoglobin e. Myoglobin serves as an oxygen storage protein as suggested by its hyperbolic binding of 02
3. A biochemist purified a protein from the bloodstream and determined its molecular weight under several conditions. In 8 M urea, which denatures the polypeptide chain, the molecular weight of the protein was 150,000 Da. She found that under reducing conditions the molecular weight of the protein was 75,000 Da, while under oxidizing conditions the molecular weight of the protein was 150,000 Da. Explain these results.
7. Which of the following events does NOT take place in/on the RER? a. cleavage of the signal recognition peptide b. biosynthesis of core oligosaccharides for N-linked glycosylation c. Phosphorylation of mannose to give rise to mannose-6-phosphate. d. attachment of a core oligosaccharide to protein via asparagine residues e. cleavage of GTP by SRP receptor

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