1. Why a peptide bond can't rotate freely? 6%.2. Theandare two amino acids usually will break an a helix. 4%3. The main force to keep a helices or 3 pleated sheets in their conformation is4%

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Answered: 1. Why a peptide bond can't rotate…

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 4RQ: Dehydration synthesis leads to formation of monomers polymers water and polymers none of the above

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The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices unwind. c. sheet structures unfold. d. tertiary structure is changed. e. quaternary structures disassemble.
Dehydration synthesis leads to formation of monomers polymers water and polymers none of the above
Steroids are among the lipids with no _________. a. double bonds b. fatty acid tails c. hydrogens d. carbons
7. Native conformation of proteins may result from: a) hydrophobic interactions b) H-bonds c) ionic bonds d) covalent bonds e) all a-d may contribute to native conformation
The β-Sheet is formed mainly by a. hydrophobic interaction b. hydrogen bonding between the peptide bond and water c. hydrogen bonding between two strands d. hydrogen bonding of the side chains e. disulfide bonding
4. Which best describes the contribution of quaternary (4’) structure of polypeptides to the native conformation of proteins: a) Structure that results from intrachain interactions of amino B) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence acid side chains of amino acids from beginning to end of molecule
3. Which best describes the contribution of tertiary (3’) structure of to the native conformation of polypeptides and proteins: a) Structure that results from intrachain interactions of amino acid side chains b) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence of amino acids from beginning to end of molecule
1. Explain how each primary structure of a protein affects its properties and how denaturation changes the structure. 2. Explain how each secondary structure of a protein affects its properties and how denaturation changes the structure.
True / False: β-bends can link together α-helices and β-sheets.
Fill in the following with the specific bond(s): Maintain(s)the helical structure of many proteins____________: ;link(s) polypeptide chains and can cause proteins tobend:_______ and________ ; join(s) the twostrands of the double helix of DNA:_________ ; link(s) amino acids to form the primary structure of proteins:_______.
Choose the best statement regarding the R groups of amino acids in an alpha helix. Group of answer choices They are located in the interior of the helix. They stick out from the axis of the helix. They participate in H-bonds that stabilizes the helix. They are completely incompatible with helix formation.
3c) The 3 structure of a protein incorporates any 2 structure the protein has, but results primarily from interactions between amino acid side groups. Name two different amino acids whose side groups could participate in each type of interaction given below under physiological conditions (pH 7.2-7.5). Ionic bonding: Hydrophobic clustering: Hydrogen bonding:

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1. Why a peptide bond can't rotate freely? 6%. 2. The and are two amino acids usually will break an a helix. 4% 3. The main force to keep a helices or B pleated sheets in their conformation is 4%.