BIOCHEMISTRY
9th Edition
ISBN: 2818440090622
Author: BERG
Publisher: MAC HIGHER
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Question
Chapter 2, Problem 13P
Interpretation Introduction
Interpretation:
The term side chain in amino acids or protein structure needs to be explained.
Concept introduction:
Amino acids are organic compounds containing amino as well as
Here, R group is different for different amino acids. This group can be acidic, basic or neutral.
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Draw any pentapeptide. All C-O, C-N, and C-S bonds must be written out, as well as all N-H, S-H, and O-H atoms/bonds. Your peptide must include at least one amino acid from each of the major classes of amino acids (i.e. charged, polar, etc.). Circle each peptide bond in this peptide.
Alpha-helix of proteins, its characteristics. Draw a diagram of the arrangement of amino acids in the alpha helix. Examples of proteins formed mainly by this structure.
Long explanations are not needed. Answers and brief descriptions would be enough.
During the formation of the peptide bond which of the following takes place?
a. Hydrogen atom is lost from its carboxyl group of one amino acid and a hydrogen atom is lost from the amino group of another amino acid.
b. Hydrogen atom is lost from its carboxyl group of one amino acid and a hydroxyl group is lost from the amino group of another amino acid.
c. Hydroxyl group is lost from its carboxyl group of one amino acid and a hydroxyl group is lost from the amino group of another amino acid.
d. Hydroxyl group is lost from its carboxyl group of one amino acid and a hydrogen atom is lost from the amino group of another amino acid.
Chapter 2 Solutions
BIOCHEMISTRY
Ch. 2 - Prob. 1PCh. 2 - Prob. 2PCh. 2 - Prob. 3PCh. 2 - Prob. 4PCh. 2 - Prob. 5PCh. 2 - Prob. 6PCh. 2 - Prob. 7PCh. 2 - Prob. 8PCh. 2 - Prob. 9PCh. 2 - Prob. 10P
Ch. 2 - Prob. 11PCh. 2 - Prob. 12PCh. 2 - Prob. 13PCh. 2 - Prob. 14PCh. 2 - Prob. 15PCh. 2 - Prob. 16PCh. 2 - Prob. 17PCh. 2 - Prob. 18PCh. 2 - Prob. 19PCh. 2 - Prob. 20PCh. 2 - Prob. 21PCh. 2 - Prob. 22PCh. 2 - Prob. 23PCh. 2 - Prob. 24PCh. 2 - Prob. 25PCh. 2 - Prob. 26PCh. 2 - Prob. 27PCh. 2 - Prob. 28PCh. 2 - Prob. 29PCh. 2 - Prob. 30PCh. 2 - Prob. 31PCh. 2 - Prob. 32PCh. 2 - Prob. 33PCh. 2 - Prob. 34PCh. 2 - Prob. 35PCh. 2 - Prob. 36PCh. 2 - Prob. 37P
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- PRACTICE NAMING. Identify the number of amino acids, number of peptide bonds, and name the peptide. i.e. Ala-Cys • Dipeptide • 1 peptide bond • Alanylcysteine Cys-tyr-phe-gln-asn-cys-pro-arg-glyarrow_forwardA peptide bond... is a version of an ester bond is a version of an amide bond is the basis of protein secondary structure is formed by addition of waterarrow_forwardThis is DNA. Locate the nitrogen bases (nitrogens are blue). Where are they located in the molecule?Locate the sugars and phosphates, and describe their location. Adjacent nucleotides are linked by covalent phosphodiester bonds (-O-P-O-) produced by a condensation reaction. What parts of the adjacent nucleotides are linked by phosphodiester bonds?Two nitrogenous bases extending towards the middle of the double helix. Are there any covalent bonds between these bases?If there are no covalent bonds between these bases, what other kinds of bonds might hold the two strands of the double helix together?arrow_forward
- Be sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Thr, Phe, Ile (2 equiv), Asp, Cys, Val, Leu, and forms the following fragments when partially hydrolyzed with HCl: Thr-Ile-Phe, Phe-Ile-Asp-Val, and Asp-Val-Cys-Leu.arrow_forwardBe sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Lys, Pro, Tyr, Ile (2 equiv) , Gln, Trp, Phe, and forms the following fragments when partially hydrolyzed with HCl: Lys–Ile-Phe-Pro, Phe-Pro-Gln-Tyr, and Trp-Ile-Lys.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
- Peptide bond properties. How these properties determine the three-dimensional structure of the protein.arrow_forwardShape and dimension. (a) Tropomyosin, a 70-kDa muscle protein, is a two-stranded α-helical coiled coil. Estimate the length of the molecule. (b) Suppose that a 40-residue segment of a protein folds into a two-stranded antiparallel β structure with a 4-residue hairpin turn. What is the longest dimension of this motif?arrow_forwardCould you please help me with this question? I am struggling. Thanks in advance. Describe the four levels of protein structure: primary, secondary, tertiary, and quarternary.arrow_forward
- Amino acid isomerism (name types). Isomerism of the carbon skeleton of amino acids - give a few examples.arrow_forward7 Protein structure.Circle one of the three amino acid sequences that is most likely to form a stable a-helix? RASKTARQ DASKTAEQ KPGKPAGQ In one sentence (that can be accompanied by a small picture) explain why?arrow_forwardPeptides. 1. Draw the peptide Ala-Glu-Gly-Lys, as it would occur at physiological pH = 7.4. The R groups of Ala and Gly are not acidic or basic, therefore do not have a pka and the charge on these R groups is therefore independent of pH. Glu is acidic and Lys is basic, therefore the charge on these amino acids is pH dependent. The pKas are shown below. pKa N-term = 9.0 C-term = 3.5 Glu4.1 Lys = 10.5 2. Draw a circle around the peptide bonds. 3. Label the C-terminus and the N-terminus. 4. What is the overall charge on the peptide at pH 7.4?arrow_forward
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