What is the charge of the primary structure of proteins at pH = 2.0, 4.0,6.0and 11.0 of the following proteins. Draw their structures and predict their net1.charge.A) Lys- Gly- Ala- GlyB) Lys- Gly-Ala-GluC) His- Gly- Ala- GluD) Glu- Gly- Ala -GluE) Gln-Gly-Ala-Lys2. Calculate the pI of the following primary structure of protein3. the migration toward the cathode, the negative pole; A for the migration towardthe anode, the positive pole; and o if the peptide remains stationary.

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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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Proper folding is essential for most proteins to function. Which of the following statement about protein folding are correct. There may be more than 1 right answer. a) changing the primary sequence will change the final conformation b) desaturation results in a protein that has a higher free energy than the native conformation c) protein spontaneously fold into their correct shape d) denatrutation will cause a protein to lose its tertiary structure
A) List each of the five major functional classes of proteins. B) Discuss the function for each class, give an example of a protein for each class and mention how the function of the protein example fits the function of the class (40 words or less for each class with its example
Φ and ψ in the Ramachandran plot (below) are: a) Rotational angles around the bond between the α-carbon and N-H (Φ) and C=O (ψ). b) Amino acid solubility in octanol (Φ) and water (ψ). c) Hydrogen bond angles in α-helices (Φ) and β-sheets (ψ). d) Amino acid solubility in water (Φ) and octanol (ψ).
Imagine you were able to incorporate real and artificial amino acids with the following side chains into proteins. Which of these would be most likely to be found buried in the interior of the hemoglobin protein in its folded form at ~pH 7.0? a) -phenol (phenyl with -OH) b) -CH2CH3 c) -phenyl d) -CH2OH
1. Which peptide would be more soluble at pH 7.0, (Val)₂₀ or (Asp)₂₀ ? at pH 3.0, (Gly-Glu-Val)
Valine is an amino acid with a nonpolar side chain and serine is one with a polar side chain. Draw the two amino acids.(a) Why is the side chain for valine nonpolar, whereas the side chain for serineis polar?(b) Which amino acid has a hydrophilic side chain and which has a hydrophobic sidechain?
in determining the structure of a fully folded protein? involving the amino acid side chains of the polypeptide. Which has the largest effect 5. hydrogen bonding ionic interactions a) b) c) d) hydrophobic interactions van der Waals interactions none of the above The misfolded, insoluble, and aggregated proteins characteristic of Alzheimer's disease and Parkinson's disease are known as: zymogens b) c) d) e) open quaternary structure proteins protein domains amyloid deposits molecular chaperones 6.
What is the molecular basis for the observation that the overall charge on a protein becomes increasingly positive as pH drops and more negative as pH increases?
Which of the following statements are False? (i) Parallel b-sheets characteristically distribute hydrophobic side chains on both sides of the sheet, and antiparallel B-sheets are usually arranged with all their hydrophobic residues on one side of the sheet. (ii) Planarity of the peptide bond means that no rotation occurs about the N-Ca bond while rotation is allowed about the C(O)-N and Ca-C(O) bonds. (iii) Silk fibers consist of fibroin proteins consisting of alternating A and G or S residues. (iv) If an aspartic acid residue were present in the interior of a globular protein, it would most likely be deprotonated and thus negatively charged.
1. Isoelectric point of polypeptide: (1) is pH at which the o-carboxyl and o-amino groups are uncharged. (2) is pH at which the net charge on the molecules in solution is 0. (3) is pH at which the charge of the o-carboxyl group is higher than the charge of the o- amino group. А. (1) only В. (2) only С. (3) only D. (1) and (3) E. (2) and(3)
Which of the following types of molecular interactions play a role in protein folding? Select all that apply. A.)Hydrophobic interactions B.)Van der Waals attraction C.)Hydrogen bonds D.)Covalent bonds
How do the following noncovalent interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could giverise to each interaction.(a) Hydrophobic interactions(b) Salt bridges (ionic interactions)

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1. What is the charge of the primary structure of proteins at pH = 2.0, 4.0,6.0 and 11.0 of the following proteins. Draw their structures and predict their net charge. A) Lys- Gly- Ala- Gly B) Lys- Gly-Ala-Glu C) His- Gly- Ala- Glu D) Glu- Gly- Ala -Glu E) Gln-Gly-Ala-Lys