Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Chapter 6, Problem 2P
Interpretation Introduction
Interpretation:
Whether the two proteins are related evolutionarily when their amino acid sequences are only
Concept introduction:
Proteins are the
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Shape 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?
Beta folding. Parallel and antiparallel beta folding sheets (be able to draw). Beta loops. Examples of proteins formed mainly by this structure.
Peptide bond properties. How these properties determine the three-dimensional structure of the protein.
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- 7 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_forwardHello, please help me with my assignment. Can you answer ALL QUESTIONS EXCEPT QUESTIONS 1-31. Which of the following statements is accurate regarding these protein structures?a. Proteins in a quaternary structure consist of a simple polypeptide chain.b. Interactions between the R groups in amino acids form tertiary structure.c. Secondary structures are formed by multiple polypeptide chains.d. The two types of primary structure are α- helices and β- pleated sheets. 2. What type of bonds are formed between amino acids?a. Peptide bondb. Glycosidic linkagec. Hydrogen bondsd. Ester linkages 3. Which of the following is an example of protein denaturation?a. Amino acids fold into repeating patterns due to hydrogen bonding of the peptide backbone.b. Several amino acids are joined together via peptide bonds.c. A protein binds with a substrate, lowering the activation energy of a reaction.d. A protein is exposed to extremely high heat, causing it to lose its secondary structure and be leftwith…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
- 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.arrow_forwardIonization State of Histidine.Each ionizable group of an amino acid can exist in one of two states, charged or neutral. The electric charge on the functional group is determined by the relationship between its pKa and the pH of the solution. This relationship is described by the Henderson-Hasselbalch equation. 1.Histidine has three ionizable functional groups. Write the equilibrium equations for its three ion-izationsand assign the proper pKa for each ionization. Draw the structure of histidine in each ionization state.What is the net charge on the histidine molecule in each ionization state? 2.Which structure drawn in (1) corresponds to theionization state of histidine at pH 1, 4, 8, and12?Note that the ionization state can be approximated by treating each ionizable group independently. 3.What is the net charge of histidine at pH 1, 4, 8, and 12? For each pH, will histidine migrate to-ward the anode (+) or cathode (-) when placed in an electric field?arrow_forwardNo plagiarism please. Use your own words. Thanks. Discuss the preferred locations of different classes of amino acids in transmembrane proteins. Explain the formation of thioether-linked prenyl anchor proteins. Explain the structure of caveolae.arrow_forward
- 11:14 structure. They provide the matrix or ground substance of extracellular tissue spaces in which collagen and elastin fibers are embedded. Hyaluronic acid, chondroitin 4-sulfate, heparin, are among the important glycosaminoglycans. 10. Glycoproteins are a group of biochemically important compounds with a variable composition of carbohydrate (1-90%), covalently bound to protein. Several enzymes, hormones, structural proteins and cellular receptors are in fact glycoproteins. Chapter 2: CARBOHYDRATES SELF-ASSESSMENT EXERCISES I. Essay questions 1. Define and classify carbohydrates with suitable examples. Add a note on the functions of carbohydrates. 2. Describe the structure and functions of mucopolysaccharides. 3. Give an account of the structural configuration of monosaccharides, with special reference to glucose. 4. Discuss the structure and functions of 3 biochemically important disaccharides. 5. Define polysaccharides and describe the structure of 3 homopolysaccharides. III. Fill…arrow_forwardNeed help. Which one of the following statements is FALSE? Group of answer choices A.Beta-pleated sheets are part of the secondary structure of proteins B.The nitrogenous bases of DNA are located on the inside because they are hydrophobic in character C.The peptide bond is formed by dehydration synthesis D.Alpha helices are stabilized by attraction between the amino acid R groups E.The peptide bond is rigid and planar and has partial double bond characterarrow_forwardQuestion 8 Review translation. Match the term and its description. Each term can only be used once. This site holds the tRNA that carries the growing polypeptide chain | Choose ) This site holds the tRNA that carries the next amino acid to be | Choose J added to the chain This site is the exit site, where discharged tRNAS leave the [ Choose ) ribosome Initiation, elongation and termination | Choose J >arrow_forward
- 2. Subunit Composition of a Protein. A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography ( F). When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol (=), three bands are again formed, this time with molecular masses of 160, 90, and 60 kDa. Determine the subunit composition of the protein. Note: dithiothreitol is a reagent to beak down the disulfide bonds.arrow_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_forwardThe number of distinct protein folds in limited. Why might this be so?arrow_forward
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