K pts on 15 of 25 NOV 016 Resources Hint Submit Answer > The tertiary structure of a protein is stabilized by several types of interactions between side chains. Classify the highlighted interaction (or bond) in each example. © Macmillan Learning Electrostatic interaction (ionic bond) Hydrogen bond Answer Bank OH -CH,C=O HỌ CH; 0 -CH,-NHO-C-CH, Hydrophobic interaction CH3 H3C CH CH CH3 H₂C Disulfide bond -CH2-S-S-CH2- м IZA ACOI Σ 00 zoom

please answer question 4 and 5

The chemical structure of cysteine (C3H-NO₂S) is shown below. Highlight each atom that is in an amino group. :S H | HC-H H-C | H-N-H :0: || C. -0-H X 5 Save For Late

5.Indicate the amino acid as polar or nonpolar OH CH: 0 H₂N-C-C-OH H O CH, 0 !! H₂N-C-C-o H CH3 CH3 CH CHO 11₂N-C-C-07 H 6) Acids and bases denature a protein by disrupting A) peptide bonds and ionic bonds. B) amide bonds and alkene bonds. C) hydrophobic interactions and peptide bonds. D) ionic bonds and hydrophobic interactions. E) ionic bonds and hydrogen bonds. 5) Heat denatures a protein by disrupting A) ionic bonds and peptide bonds. B) hydrophobic bonds and hydrogen bonds. C) peptide bonds and hydrophobic bonds. D) disulfide bonds and peptide bonds. E) hydrogen bonds and disulfide bonds. 7) Denaturation of a protein A) changes the primary structure of a protein. B) disrupts the secondary, tertiary, or quaternary structure of a protein. C) is always irreversible. D) hydrolyzes peptide bonds. E) can only occur in a protein with quaternary structure. 8) Heavy metals denature proteins by A) releasing amino acids. B) disrupting hydrophobic interactions. C) changing the pH of the…

Give detailed Solution with explanation needed..don't give Handwritten answer

Modify isoleucine to show its structure at pH 1 and pH 13. Modify each amino acid by adding or removing atoms or bonds and by adding charges where appropriate. pH 1 pH 13 Draw Rings More Erase Select Draw Rings More Erase C O |||||| C CH₂ | CH₂ 1 Select / |||||| H₂C H₂N 5 C - | CH H N H Q2 Q CH₂ | CH₂ | H₂C - CH H₂N — — H H O H N - H ✪ 2 Q

Given below is the structure of a peptide with the name seryllysylaspartate. What is the amino acid at the C-terminus (or C-terminal amino acid) of this peptide? OH | CH, O || + H₂N-C | H O lysine Z-: serine + ŃH₂ T CH₂ T O aspartate CH₂ T CH₂ CH, O || N -C | O lysylaspartate H H C CH, O || C-O C-N C 1 H H

3. study the Lewis structure of a geheric amino acial shann below ldentify the part af generic amino acid that reacts ith bose and the part thadthaanctawith acial. Brief explain your ansher R C-COOH NH

The tertiary structure of a protein is stabilized by several types of interactions between side chains. Classify the highlighted interaction (or bond) in each example. Answer Bank Hydrogen bond OH -CH,-C=O…HO-CH, Electrostatic interaction (ionic bond) 요 -CH,-NH, O-C-CH, OC-CH Hydrophobic interaction CH3 H3C -CH CH- CH, HẠC Disulfide bond -CH₂-S-S-CH₂-

© Macmillan Learning 0 Resources Solution Penalized ? Hint Submit Answer Name the tripeptide using the three letter amino acid abbreviations separated by a hyphen. (For example: Gly-Ala-Phe). H =O C -C-C name: -C-O CH₂ CH2 CH2 CH2 H3C-CH OH C=O CH3 How many peptide bonds are in this structure? peptide bonds: 2 Attempt 3