(a)
To determine: A single amino acid from each pair which is more likely to be found in the interior of the protein molecule. The pairs are as follows:
- Alanine; glycine.
- Glutamate; aspartate.
- Tyrosine; phenylalanine.
- Methionine; cysteine.
Introduction: The protein is the building block of the body. The long chains of amino acids are joined together by means of “peptide bonds.” The process of synthesis of proteins takes place by the process of translation which uses a “template strand” in the synthesis of protein strands. The mRNA guides the synthesis of the protein molecules.
(b)
To explain: The localization of cysteine residues with free sulfhydryl groups on the exterior surface of the protein molecule and the presence of cysteine molecules with disulfide bonds to the interior side of the protein.
Introduction: The protein is the building block of the body. The long chains of amino acids are joined together by means of “peptide bonds.” The process of synthesis of proteins takes place by the process of translation which uses a “template strand” in the synthesis of protein strands. The mRNA guides the synthesis of the protein molecules.
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Becker's World of the Cell (9th Edition)
- Rotation about the peptide bond in glycylglycine ishindered. Draw the resonance forms of the peptide bondand explain why.arrow_forwardInstruction for the said activity: Write the structure of each of the following peptide at pH7 and identify how many peptide bond in each number. d. Alanyl-phenylalanine- aspartate- cysteine e. Threonyl- Isoleucyl-methionyl- leucine f. Lysyl-alanine -Phenylalanyl-tyrosyl- serinearrow_forwardThe polarity if the solvent and other environmental factors can affect the pKa of a weak acid. Suppose that the amino group of a protein has a pKa of about 8.0 when exposed to water on the outside of a protein. (a) Would you expect the pKa to be higher or lower than 8 if the group were buried in the hydrophobic interior of a protein? Explain. (b) Suppose that the hydrophobic interion of the protein contains a carboxylate side chains of an Asp residue in close proximity to the amino group. What would you now expect for the pKa of the amino group?arrow_forward
- Drawing the Structure of a Glycopeptide (Integrates with Chapters 4and 5.) Consider the peptide DGNILSR, where N has a covalentlylinked galactose and S has a covalently linked glucose. Draw thestructure of this glycopeptide, and also draw titration curves for theglycopeptide and for the free peptide that would result from hydrolysis of the two sugar residues.arrow_forwardSweet proteins. List the key classes of glycoproteins, their defining characteristics, and their biological functions.arrow_forwardcotton. Which aspect of the structure of cellulose accounts for its strength? Cellulose is an abundant structural polysaccharide found in plant cell walls, wood, and interchain hydrogen bonding between extended molecular chains repeating unit of N-acetylglucosamine a(1→4) linkages between glucose units branches that occur every 12-30 residues forms a helical conformation in water Which of the following is not correct about chitin? fundamental constituent of the exoskeletons of crustaceans, insects, and spiders b) chitin chains form extended ribbons that pack side-by side a) similar to cellulose but with repeating units of N-acetyl-D-glucosamine c) d) found mainly in the liver in humans, making up as much as 10% of liver mass stacked sheets of chitin strands are stabilized by intrastrand, interstrand, and intersheet hydrogen bondsarrow_forward
- Correlation between lipid profile and Covid-19.Explain this statement.arrow_forwardpeptide Lys-Glu-Trp answer the following questions: Draw the structure of this peptide when all the ionizable groups are fully protonated. How many ionizable groups does this peptide have? Label the pKa for each of the ionizable groups in the structure above. Draw the appropriate titration curve for this peptide on graph paper starting at pH 0 and ending at pH 14. Label the x-axis, y-axis and the pKa Determine the overall net charge of this peptide at each full equivalent point (including 0) where the ionizable group is 100% deprotonated. Determine the pI for this peptide. Determine the average overall net charge of a mixture of this peptide in a solution where pH=8.5.arrow_forwardComponents of Complex Biomolecules Figure 1-10 (Lehninger's Biochemistry book) shows the major components of complex biomolecules. For each of the two important biomolecules below (shown in their ionized forms at physiological pH), identify the constituents. And show H-bonding with water. (a) Guanosine triphosphate (GTP), an energy-rich nucleotide that serves as a precursor to RNA: N- NH -CH2 0- NH2 H H H H. ОН ОН (b) Phosphatidylcholine, a component of many membranes: CH3 O- CH3*N-CH2-CH2-0-P-0–CH2 нн CH3 НС —О—С—(CH), —С—С— (CH), — СHз CH,–0-C-(CH,)14–CH3arrow_forward
- Activity: Write the line structure of each of the following peptide at pH7 and identify how many peptide bond in each number. 1. Glycyl-valyl-serine 2. Threonyl-cysteine 3. Isoleucyl-methionyl-aspartatearrow_forwardAla-Arg-Val-His-Asp-Gln Given the polypeptide chain above Estimate the net charge of the polypeptide chain at physiological pH (7.4) and at pH 5.0 . How many peptide bonds are there? What kind of polypeptide is it?arrow_forwardPeptide sequence using 1-letter code for amino acids: EDLSMTCFRH What is the net charge of this peptide at pH 9? Use the pKa values from Table 4-1 from Voet, Voet and Pratt. -2 -1 O +1 +2arrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning