6. In synthetic polyethene -(CHXCH2)n- has a random coil structure. Here (CHXCH2)- refers to its primary structure and random coil structure is the secondary structure
7. Both the ?-helix and the ß-sheet referes to the secondary structure of the proteins.
8. A-T and G-C
2. Problem done in image
The synthetic polyethene, -(CHXCH_2) -, has a random coil structure. Here, (CHXCH_2) refers to its ____...
Some regions of protein secondary structure are described as "random coil". This designation is misleading because: A. the secondary structure must always be an alpha helix or beta sheet. B. although the structure is indeed random, it need not necessarily resemble a "coil". C. although the region may be unique to a particular protein, it is not random: each cellular copy of that protein will contain an identical "random coil" structure that corresponds to the same portion of primary sequence....
9. Alpha-helices and B-pleated sheets are both examples of a. primary structure. b. secondary structure. c. tertiary structure. d. quaternary structure. 14. The most common moti uispersion forces nost common motifs for this level of structure are the helix and the B- pleated sheet a. primary structure b. secondary structure c. tertiary structure d. quaternary structure e. both secondary and tertiary of a protein. 15. The amino acid sequence is the a. primary structure b. secondary structure c. tertiary structure...
55) a major molecule of the cell contains the atoms, C, N, O, and it may be protein carbohydrate lipid nucleic acid and d An example of protein secondary structure is (are): b) whatchamacallit alpha helix fibrous globular none of the above The structure of the alpha helix is maintained by: b) covalent bonds ionic bond hydrogen bonds personal bonds stocks and bonds 58) The protein beta sheet is an example of primary structure secondary structure tertiary structure quaternary structure...
Classify each protein example according to its highest level of protein structure. Primary structure Secondary structure Tertiary structure Quaternary structure myoglobin with heme thethe C helix of α-lactalbumin Gly-Ala-Val-Leu hemoglobin
(2%) Indicate which secondary structure or structures (α -helix, β -pleated, random coil) will the following peptide adopt in an aqueous solution at pH 7 (2%) The unfolding of the alpha 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-Glu residues, has the alpha helical conformation at pH 3....
2) At a pH greater than that of its isoelectric point, the structure of glycine is a) H-CH-COOH b) H-CH-C00- c) H-CH-CO e) H-CH-COO COOH b) H-CH-C00- c) H-CH-COOH d) H-CH-COO NH2 NH2 NH2 NH3 NH 3) Which of the following structures can be destroyed by the dena structures can be destroyed by the denaturation of a protein? a) Only primary and tertiary structures of a protein. b) Only secondary, tertiary y secondary, tertiary, and quaternary structures of a protein....
Indicate which secondary structure or structures (a-helix, β-pleated, random coil) will the following peptide adopt in an aqueous solution at pH 7 5. leu-Glu-Asn-Glu-GIn-Asn-Met-Ala-His-Phe-Trp-Tyr
What kinds of interactions are NOT part of tertiary protein structure? 3 . A) salt bridges In a hydrolysis reaction, B) hydrophilic interactions A. an acid reacts with an alcohol. C) disulfide bonds E. an este reacts with NaOH. C. anester reacts with H.O. D) peptide bonds D. an acid neutralizes a base. E) hydrophobic interactions E. water is added to markene. . All amino acids have chiral Carbon atoms except a. Val 6. Lys C. ASP d. Ala e....
1. Compare and contrast the structure and function of myoglobin to hemoglobin. Provide detailed information & figures on the primary, secondary, tertiary & quarternary structures pf these proteins, and how these structures reate to function. 2. Provide a detailed drawing (with figures) of the prosthetic group Heme and a detailed explanation of its role in myoglobin amd hemoglobin function. 3. Provide a detailed drawing (with figures) of the cooperative binding of oxygen by hemoglobin. 4. Provide a detailed drawing (with...
20 Marks) Question 3 a) The structure of proteins is described at four levels: primary, secondary, tertiary and quaternary Briefly explain what is referred to by each of these terms. Why are these distinctions useful? [5 marks] b) Each level of protein structure is stabilised by chemical bonds and interactions: List the bonds and/or effects primarily responsible for stabilising each level of structure. [5 marks] c) The illustration below shows a molecule of haemoglobin. Describe TWO (2) aspects of haemoglobin...