Becker's World of the Cell (9th Edition)
9th Edition
ISBN: 9780321934925
Author: Jeff Hardin, Gregory Paul Bertoni
Publisher: PEARSON
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Chapter 3, Problem 3.2PS
Stability of Protein Structure. Several different kinds of bonds or interactions are involved in generating and maintaining the structure of proteins. List five such bonds or interactions, give an example of an amino acid that might be involved in each, and indicate which level(s) of protein structure might be generated or stabilized by that particular kind of bond or interaction.
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Chapter 3 Solutions
Becker's World of the Cell (9th Edition)
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- Formation of the tertiary structure of a protein - what are the main physical forces affecting the assembly of the tertiary structure of proteins. The chemical compounds formed during the assembly of the tertiary structure of a protein.arrow_forwardDraw 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.arrow_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_forward
- Peptide bond properties. How these properties determine the three-dimensional structure of the protein.arrow_forwardLong 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.arrow_forwardProtein folding- what is the Role of chaperones and chaperonins in protein folding. The Formation of intermediate structures in the process of protein folding , explain the theory of intermediate structure. Example of Protein folding energy diagram.arrow_forward
- Proteins are quite stable. The lifetime of a peptide bond in aqueous solution is nearly 1000 years. However, the free energy of hydrolysis of proteins is negative and quite large. How can you account for the stability of the peptide bond in light of the fact that hydrolysis releases much energy?arrow_forwardFigure 7 shows one additional type of bond that can stabilize the tertiary structure of a protein. This bond is called a disulfide bond (or disulfide bridge), and it involves the sulfhydryl (-SH) R groups from one particular type of amino acid. A disulfide bond can form only under certain conditions (oxidative conditions). We'll talk about oxidation and reduction next week. For now, just note that this type of bond does exist in some proteins. Answer the below questions on tertiary structure in your own document. 8. Figure 6 shows examples of bonds that might stabilize the tertiary structure of a protein (labeled A, B, and C). Do these interactions involve only the amino acid R groups, only the polypeptide backbone atoms, or both? 9. In the table below, indicate what type of bond/ interaction is represented in the examples shown in Figure 6, panels A, B, and C and whether each interaction involves group or backbone atoms. Example Type of Bonding Interaction R group or backbone? A В 10.…arrow_forwardOptical isomerism of amino acids. L and D amino acids. Chiral centers of amino acids. Give examples of amino acids that do not have optical isomers.arrow_forward
- Hello, 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_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_forward2. 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_forward
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Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY