40.What would you expect about the formation of an alpha-helix for a segment of a proteinchain that contains lysine approximately every four residue with all other residues being mostlyhydrophobic?A. Helix formation would be favored at low pHB. Helix formation would be favored at high pHC. Helix formation would be favored at neutral pHD. Helix formation would never occur regardless of pH

Two types of secondary structures are abundant in protein: alpha helix and beta sheets. The alpha…

Answered: 40. What would you expect about the…

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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29. In sickle cell anemia, a hereditary disease, there is substitution of one amino acid by another in one of the four polypeptide chains of hemoglobin. In this case are all of the structural levels of the protein modified?
4. Let’s build a polypeptide chain a. Using your arsenal of 4 amino acids, write out the primary structure of an 8 amino acid long polypeptide that you might be called amphipathic and thus allow it to form a micelle in aqueous solution, identify amino acid 1 through 8 as well as the location of the amino and carboxy termini of the polypeptide. b. Explain why this polypeptide would be considered amphipathic and draw what the micelle might look like in water. c. Taking amino acids 3, 4, and 5, draw the molecular structure of this particular stretch of polypeptide chain. Along the backbone linkage of the polypeptide identify the peptide bonds with a PB, the bonds with free rotation FR, and bonds with limited rotation LR.
In the alpha-helices, which of the following statement is NOT true? a. Backbone carbonyl oxygen of residue (i) hydrogen bonds to backbone NH of the fourth residue of chain of residue (i + 4). b. Side chains project out from an α-helix. c. Hydrogen bonds are almost straight and parallel to the helix axis. d. Helix has a macrodipole. e. The rise or advance per amino acid residue is 0.54 nm.
Amino acid sequence in a protein that can form N-glycosylation is called a glycosylation sequon. Which of the following is such a sequon? a. Asn-Ala-Thr b. Gln-Ala-Thr c. Asn-Pro-Pro d. Asn-Ala-Ala e. Gln-Ala-Ala
in what groups can we subdivide the amino acids pick one or more A. Amino acids with polar side chains B. amino acids with acidic electrically charged side chains C. amino acid with amphipathic charge side chains D. amino acids with nonpolar side chains E.amino acids with basic electrically charged side chains What is the process of polymerization in proteins? Pick one A. Amino acids are added to a polypeptide strand B. nucleic acids are added to a polypeptide strand C. amino acids are removed from a polypeptide strand D. the cross-linking of different polypeptide strands
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
In the given structure below, 1. What protein was used as the template for modelling the structure of the assigned amino acid sequence? 2. How many alpha-helices and beta-sheets are there?
Which of the following descriptions best describes the composition of nucleotides? Group of answer choices A. a pentose sugar and a purine or pyrimidine B. a nitrogenous base, a phosphate group, and a pentose sugar C. a nitrogenous base and a pentose sugar D. a nitrogenous base and a phosphate group E. a phosphate group and an adenine or uracil
Which of the following amino acid or types of amino acids are are rarely found in beta sheets? a. Polar charged amino acids b. Polar uncharged amino acids c. Non polar amino acids D. Glycine
9.2
Which of the following is incorrect about the beta-sheet? a. The strands in anti-parallel beta-sheets are usually connected with turns b. Side chains are alternated above and below the sheet C. Parallel beta-sheets are less stable than the anti-parallel ones Od. It is stabilized by hydrophobic interactions between the side chains of nonpolar residues
Most proteins denature at high temperatures. A. Are peptide bonds typically broken at high temperatures, yes or no? _________________ B. Does denaturation disrupt the primary structure of a protein, yes or no? __________________ C. Why do proteins denature at high temperatures? D. Is it likely that a denatured protein is able to perform its physiological function, yes or no? Why or why not? Thoughtfully defend your answer.

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