Choose the CORRECT statement. O A polypeptide chain may have abrupt changes in direction and restriction in geometry because of the presence of glycine O A polypeptide chain may have abrupt changes in direction and restriction in geometry because of the presence of valine O A polypeptide chain may have abrupt changes in direction and restriction in geometry because of the presence of arginine O A polypeptide chain may have abrupt changes in direction and restriction in geometry because of the presence of proline

Choose the CORRECT statement. O A polypeptide chain may have abrupt changes in direction and restriction in geometry because of the presence of glycine O A polypeptide chain may have abrupt changes in direction and restriction in geometry because of the presence of valine O A polypeptide chain may have abrupt changes in direction and restriction in geometry because of the presence of arginine O A polypeptide chain may have abrupt changes in direction and restriction in geometry because of the presence of proline

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter3: Biological Macromolecules

Section: Chapter Questions

Problem 10RQ: Lactose is a disaccharide formed by the formation of a bond between glucose and glycosidic; lactose...

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GABA (B) Need help answering these questions about the GABA(B) protein.  What class (globular, fibrous, membrane) protein is the protein Identify the organism (or organisms that have this protein) Identify the cellular location of this protein Describe the function Find the primary structure (list it on a slide) Describe secondary structure (alpha-helix, beta sheet, and how many of each and what percent of the total protein) Find a picture of the tertiary structure (which should also show secondary structure) Does the protein have a quaternary structure, if so what is it?
Which of the following statements are TRUE? Multiple answers:Multiple answers are accepted for this question PLEASE SHOW WORK FOR EACH PART AND EXPLAIN WHY EACH ANSWER CHOICE IS WRONG OR RIGHT a. The tripeptide His-Lys-Glu has a net charge of -2 at pH 8.0. b. The tripeptide Asp-Asp-Asp has a net charge of -3 at pH 7.0. c. The tetrapeptide His-His-His-His has a net charge of -1 at pH 7.0. d. There are 6 possible sequences for a tripeptide containing Arg - His - and Pro. e. Certain bacteria synthesize cyclic tetrapeptides. The net charge at pH 7.0 of a cyclic tetrapeptide consisting of two Pro and two Tyr is 0.
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.
Question 9. Which of thefollowing is not formed through adehydration synthesis reaction?A. polysaccharideB. polypeptideC. Nucleic acidD. phospholipidE. glycerol
Lactose is a disaccharide formed by the formation of a bond between glucose and glycosidic; lactose glycosidic; galactose hydrogen; sucrose hydrogen; fructose
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
Please help me with this question. More than one answer may be correct. Elastin _______. Options: A) has a repeating structure of 3 amino acids such as Gly-Pro-X B) crosslinks with numerous other elastin peptides to make an elastic fiber C) is physically attached to the smooth endoplasmic reticulum D) is physically attached to ribosomes E) is rich in hydrophobic residues
Unsaturated fatty acids have ----. Question 16 options: multiple amide groups in their hydrocarbon chain. one or more double bonds in their long hydrocarbon chain. one or more single bonds in their long hydrocarbon chain. multiple aldehyde groups in their long hydrocarbon chain.
4 This is a three-part question about a tripeptide. Answer all three sub-questions. The pKR of side chains of Tyr, and Lys is 10.46 and 10.54 respectively. The molecular weight of amino acids Ala, Lys, and Tyr in neutral form is 89.1, 146.2, and 181.2 Da, respectively. 1) Draw the chemical structure of the dominant form of tripeptide AKY at pH = 11.5, ensure you have the correct stereochemistry and ionization state of each functional group (Hint, lysine has a C-epsilon as the furthest carbon from C-alpha). 2) Calculate the pI of tripeptide AKY, assuming the terminal amino group has a pKa of 8.0, and the terminal carboxyl group has a pKa of 3.5 3) Calculate the molecular weight of AKY at pI
How can IDPs can gain a stable conformation? Question 45 options: By interacting with other proteins. They already exist in their final structure due to protein folding. By interacting with partially folded intermediates. By testing multiple partially stable intermediate structures to find the most energetically favourable structure
BIOMOLECULES - Please answer the questions properly. - Multiple choice 1. Chymotrypsin is a digestive enzyme that breaks down proteins. From the following attributes, which one does not characterize chymotrypsin? A. A thiol nucleophile B. Performs proteolysis C. A tetrahedral intermediate D. A catalytic triad of serine, histidine, and aspartate 2. Evaluate the secondary structure of proteins. Which of the following differentiates alpha structures to those beta structures? ? A. alpha structures are helices and beta structures are pleated sheets B. alpha structures are primary and beta structures are secondary C. alpha structures are parallel and beta structures are antiparallel D. alpha structures are L and beta structures are D