Within a polypeptide chain is the following amino acid sequence, which reads in the N terminus to C terminus direction from left to right: Glycine-Tyrosine-Serine. Which statement about this polypeptide is true? The side chains or R groups of the amino acids in the sequence are covalently bonded to one another through peptide bonds. A condensation reaction formed a peptide bond between the amino group of glycine and the carboxyl group of tyrosine. A molecule of water was released when the carboxyl group of tyrosine formed a peptide bond with the amino group of serine. A hydrolysis reaction occurred during peptide bond formation between the carboxyl group of glycine and the carboxyl group of tyrosine. The polypeptide can become branched if the side chain of tyrosine reacts with a free amino acid to form a peptide bond.

Within a polypeptide chain is the following amino acid sequence, which reads in the N terminus to C terminus direction from left to right: Glycine-Tyrosine-Serine. Which statement about this polypeptide is true? The side chains or R groups of the amino acids in the sequence are covalently bonded to one another through peptide bonds. A condensation reaction formed a peptide bond between the amino group of glycine and the carboxyl group of tyrosine. A molecule of water was released when the carboxyl group of tyrosine formed a peptide bond with the amino group of serine. A hydrolysis reaction occurred during peptide bond formation between the carboxyl group of glycine and the carboxyl group of tyrosine. The polypeptide can become branched if the side chain of tyrosine reacts with a free amino acid to form a peptide bond.

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section: Chapter Questions

Problem 9TYU: Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary...

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Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.
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A portion of a polypeptide chain contains the following sequence of amino acids: (-Met, -Leu, -Ala, -Cys, -Asp-) a.) Which amino acid can form a disulfide bond? b.) Which amino acids are likely to make the polypeptide more soluble in water? c.) Which amino acids are likely to make the polypeptide less soluble in water? d.) How does the primary structure of a protein affect its tertiary structure?
The structure of an alpha helix orients the oxygens of the carbonyl group of the peptide bond towards the C-terminal end of the helix while the hydrogens of the NH groups orient toward the N-terminal end, thus imparting a dipole along the length of the helix. As a result, which kinds of amino acids would favor the C-terminal end, and which would favor the N-terminal end? negatively charged, positively charged positively charged, negatively charged negatively charged, hydrophobic positively charged, hydrophobic hydrophobic, negatively charged hydrophobic, positively charged
A peptide with the sequence isoleucine1-aspartate2-valine3-lysine4-proline5-glutamate6 is located at the surface of a protein. Which residues are likely oriented toward the interior of the protein and what is the most likely secondary structure that this peptide is in? a.) Residue numbers 2, 4, 6; alpha helix b.) Residue numbers 1, 3, 5; alpha helix c.) Residue numbers 1, 3, 5; beta sheet d.) Residue numbers 2, 4, 6; beta sheet
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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?
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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
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