Serine and threonine can both be directly deaminated during amino acidmetabolism. What else do these two amino acids have in common?Both are achiral hydrophobic amino acids.Both can be phosphorylated or glycosylated.Both destabilize beta sheets if they are incorporated into the secondarystructure.Both readily form covalent disulfide bonds to stabilize a protein's tertiarystructure.

The building components of proteins are amino acids. They are organic compounds made composed of a…

Answered: Serine and threonine can both 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

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Which of the following amino acids would you expect to find more often near the center of a folded globular protein? Which ones would you expect to find more often exposed to the outside? explain your answers. Ser, Ser-p (a Ser residue that is phosphorylated), Leu, Lys, Gln, His, Phe, Val, Ile, Met, Cys–S–S–Cys (two cysteines that are disulfide- bonded), and Glu. Where would you expect to find the most N-terminal amino acid and the most C-terminal amino acid?
Which of the following statements best describes the hydrophobic character of bacteriorhodopsin (2BRD)? Both the interior and exterior of the protein are hydrophobic, including the central core of the trimer. Both the interior and exterior of the protein are hydrophilic, including the central core of the trimer. Both the interior and exterior of the protein are hydrophilic, but the central core of the trimer is hydrophobic. Both the interior and exterior of the protein are hydrophobic, but the central core of the trimer is hydrophilic.
Most animals cannot use wool for nourishment. An exception is the clothes moth: it can derive nourishment from eating clothing made of natural fibers such as wool (which is rich in a-keratin). The digestive tract of the larvae of clothes moths provides a highly reducing environment. Why is this beneficial to the larvae? The reducing environment will reduce the disulfide linkages, making it easier to digest the proteins. The reducing environment will hydrolyze the peptide bonds. The reducing environment will interfere with the H-bonding between the tropocollagen molecules, making the type of protein found in most natural fibres easier to digest. The reducing environment will help to kill bacterial pathogens. The reducing environment will detoxify the carcinogenic dyes used in the textile industry.
13) Like beans, eggs would be most likely to be deficient in at least one essential amino acid. True or False 14) There are hydrophilic interactions between the following R groups in the tertiary structure of a protein. True or False -CH2 CO- and -CH2CH2CH2CH2NH3+ 15) In digestion, proteins are broken down into amino acids in a hydrolysis reaction. True or False 16) The ionized form of all ami o acids at physiological pH (7.4) has a net charge of zero. True or False
Sketch a titration curve for the following amino acids and indicate the pKa values for all titratable groups. Also indicate the pH at which this amino acid has no net charge. aspartic acid gly-val
Which of the following amino acids would you least expect to find on the surface of a water-soluble protein? Explain I Serine Glutamat Lysime Threonine
Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln How does trypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end. List down the different fragments that would result if dynorphin were cleaved by trypsin. . How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. . Cyanogen bromide is a chemical reagent which also cleaves peptide bonds. What is/are…
Amino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?
Consider the peptides Pro-Gin-Val-Phe-His-Asp-Cys and His-Gln-Pro-Cys-Asp-Phe-Val. How do these two peptides differ? (Select all that apply.) The two peptides have different compositions. The two peptides have different isoelectric points. The two peptides have different titration curves. The two peptides differ in amino acid sequence. [References] If you were to have a mythical amino acid based on glutamic acid, but one in which the hydrogen that is attached to the y-carbon were replaced by another amino group, what would be the predominant form of this amino acid at pH 12 if the pK, value were 10 for the unique amino group? (Select all that apply.) Both of the carboxyl groups are deprotonated. The amino acid-carries a negative 2 charge. The amino acid carries a negative 4 charge. The amino groups are in the form -NH". Both of the amino groups are deprotonated.
The carbohydrate portion of some glycoproteins may serve as a cellular recognition site. To perform this function, the oligosaccharide moiety must have the potential to exist in a large variety of forms. Which can produce a greater variety of structures: oligopeptides composed of five different aminoacid residues, or oligosaccharides composed of five different monosaccharide residues? Explain.
Which of the choices are types of posttranslational modifications a newly synthesized protein may undergo? Select all the choices that apply. changes to hydrogen bonding capabilities formation of an amide bond between Cys and an isoprenyl group removal of prosthetic groups removal of the thiol group from a Cys residue modulation of charges on amino acids proteolytic cleavage covalent attachment of oligosaccharides to Asn, Thr, or Ser
What percentage of the a-amino group of lysine will be protonated at its pI?< 25% 50% >75%

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