### Multiple Choice Questions on Amino Acids and Proteins#### Question 27*Arginine is the most basic of the 20 amino acids because its side chain is ________ under most cell conditions.***Options:**- A. Very highly charged- B. Hydrophobic- C. Titrated- D. Protonated- E. Negatively charged#### Question 28*Concentrations of some proteins cannot be estimated by UV spectrophotometry because they are ____________.***Options:**- A. High in non-absorbing amino acids- B. Low in tryptophan and tyrosine- C. Low in protein- D. High in aromatic amino acids### Explanation:**For Question 27:**Arginine is identified as the most basic amino acid due to its side chain properties in cellular environments. The side chain is ________ (the correct option from the choices given) under physiological conditions, which contributes to its basic nature.**For Question 28:**Some proteins' concentrations cannot be accurately measured using UV spectrophotometry. This technique relies on the absorption properties of amino acids like tryptophan and tyrosine. Therefore, the inability to estimate concentrations is due to ___________ (the correct option from the choices given).

Amino acids are the monomers of proteins. These are the molecules that contain both amino and…

Answered: 27.Arginine is the most basic of the 20…

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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The side chain of which residue can be hydrogen bond donor: a. Thr b. Ala c. Ile d. Pro e. Phe
N-linked oligosaccharides can be covalently linked to proteins at which amino acid? a. Gly b. Ser c. Glu d. Tyr e. Asn
Imidazole is used to elute His6-tagged proteins from Ni-NTA resins because imidazole is: a. More acidic b. Structurally similar to histidine c. More basic d. A compound that can change the pH in the buffer
Mass spectrometry and X‑ray diffraction are common biochemical techniques for characterizing proteins. Classify each statement based on whether it applies to mass spectrometry, X‑ray diffraction, or both techniques.
4. Exhibit 4A The following question(s) refer to this peptide: Cys-Ala-Gly-Arg-Gln-Met Refer to Exhibit 4A. The overall, net ionic charge on this peptide at pH = 7 would be: A. +2 B. +1 C. 0 D. -1 E. -2
A structural difference between uracil and cystosine is: A. At C-4 cytosine has an amino group, while uracil as an oxo group B. At C-6 cytosine has an amino group, while uracil as an oxo group C. At C-4 cytosine has an amino group, while uracil as an oxo group D. Both have an oxo group at C-2 E. At C-2 cytosine has an amino group, while uracil as an oxo group
Which of the following statements is true? A. B. C. D. Peptide bonds are the only covalent bonds that can link together two amino acids in proteins. The polypeptide backbone is free to rotate about each peptide bond. Nonpolar amino acids tend to be found in the interior of proteins. The sequence of the atoms in the polypeptide backbone varies between different proteins.
2. Would you expect an instrinsically disordered protein to contain a higher proportion of hydrophilic or hydrophobic residues? Explain your reasoning.
Which factors will cause protein denaturation? Group of answer choices a. aqueous phosphate buffer b. heavy metals - Hg2+, Pb2+, Ag+ c. small metal ions - Na+, Ca2+, Cl- d. changes in pH e. use of detergents or soaps f. Tris a buffer commonly used with proteins
Which of the following compounds is most similar to the transition state of peptide bond hydrolysis? A. R2 D. R2- H HO .R1 N میں ملی B. R2 مل ما -R1 E. OH R2 C -R1
Beta-sheets are roughly planar structures, in which the backbone hydrogen bonding pattern defines the plane. Where are the side chains in a sheet? Select one: a. The side-chains are on the outside of the sheet. O b. The side-chains are in the plane of the sheet, with residues from one chain on one side of the sheet, and residues from the other chain being on the other side. The side-chains do not have a consistent pattern. d. The side-chains are perpendicular to the plane of the sheet, with residues from one chain being above and residues from the other being below the plane of the sheet. C. e. The side-chains are perpendicular to the plane of the sheet, with residues from each chain alternating between above and below the plane of the sheet. O f. The side-chains are in the plane of the sheet, with residues from each chain alternating being on one side or the other of the sheet. g. Beta-sheets are rarely observed in proteins.
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

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