38. Which results in the complex 3-dimensional folding pattern of a polypeptide? Group of answer choices interaction of more than one polypeptide chain interaction of polypeptide backbone interaction of polypeptide side chains denaturation and renaturation of proteins
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- Which of the following is a functional group that is part of a building block of proteins? phosphate adenine amino riboseGiven the polypeptide chain below: Ala-Arg-Val-His-Asp-Gln 1. What kind of polypeptide is it? 2. How many peptide bonds are there?based on this oligopeptide (KEQSCMV) would someone be able to help me on the following questions? What moieties within oligopeptide are those mainly responsible for the formation of an alpha-helix? Name the process that leads to the unfolding of the alpha helix to yield a random coil. State and justify, for oligopeptide, which amino acid side chains will be involved in: hydrophilic interactions, hydrophobic interactions, disulphide bridges and salt bridges. In each case, briefly justify your choice.
- -100 100 8. This is a helical wheel projection. The following amino acids of your protein were predicted to participate in an alpha helix: DRMVEHACKSI. a. Plot these amino acids in the helical wheel projection below. b. Is the alpha helix in your protein hydrophobic, amphipathic or hydrophobic? c. Would you expect this helix to be on the interior of the protein, exposed, or partially exposed?Figure 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.…Beta ( ? ) sheets are a type of secondary structure in proteins. A segment of a single chain in an antiparallel ? sheet has a length of 80.5 Å . How many residues are in this segment?
- β-pleated sheets and α-helices arise more from interactions in the peptide backbone than from the “R” groups of the individual monomers; they are examples of the (????) structure of a protein. Primary Tertiary Secondary Quaternary (????) are comprised of a nitrogenous base, a pentose sugar, and a phosphate group. Monosaccharides Amino acids Proteins Nucleotides (????) is the RNA transcript of the DNA sequence that determines the primary structure of a protein. mRNA lncRNA tRNA rRNA If a substance such as a lipid isn’t soluble in water it might be described as (????) Hydrophilic HydrophobicThe unfolding of the α helix of a polypeptide to a randomly coiled conformation is accompanied by a large decrease in a property called specific rotation, a measure of a solution’s capacity to rotate circularly polarized light. Polyglutamate, a polypeptide made up of only L-Gluresidues, has the α-helix conformation at pH 3. When the pH is raised to 7, there is a large decrease in the specific rotation of the solution. Similarly, polylysine (L-Lys residues) is an α helix at pH 10, but when the pH is lowered to 7 the specific rotation also decreases, as shown by the following graph. What is the explanation for the effect of the pH changes on the conformations of poly(Glu) and poly(Lys)? Why does the transition occur over such a narrow range of pH?Quaternary structure of the protein is possible for Both monomeric and multimeric protein Multimeric protein Monomeric protein All protein structures
- Given a peptide chain that is composed of the following amino acids:(branched chain-- polar uncharged--polar positively charged -- polar negatively charged-- aromatic) 10If the component amino acids of the above peptide chain are subjected to paper chromatography, which of the amino acids will be farthest from the point of origin?Part B Assume a protein is composed of 120 amino acid residues and that each amino acid can have three possible orientations. How many total possible orientations are there for the protein? Express the number of possible orientations to three significant figures. —| ΑΣΦ 1.797 • 1057 Each possible orientation of an amino acid is due to rotation about a bond. Since there are two terminal amino acids, there will be one fewer peptide bond compared to the number of amino acids. No credit lost. Try again. Submit ? Previous Answers Request Answer orientationsThe different types of interactions that stabilize the protein tertiary structure are illustrated in the diagram below. Which type of interaction moves some part of the polypeptide chain toward the inside of the folded protein? OH Hydrophilic OH CH₂ interaction with water Hydrogen bond -NH₂3-0- C Salt bridge -CH₂-OH C=0 H-N H 0-CH,- I H Hydrogen bond Salt bridge O Disulfide bond 222 -SIS Hydrophobic interaction 200 O Hydrogen bond O Hydrophilic interaction Disulfide bonds B-Pleated sheet O Hydrophobic interaction CH₂ CH₂ a Helix CH3 CH3 Hydrogen bonds