Please solve 7F1!QAAIoptionZ@ 2*F2WSProteins have complex three-dimensional structures. These polymers are heldinto these specific shapes with a variety of intermolecular forces, covalent bonds,and ionic bonds.Proteins fold into complex tertiary shapes that are held in place with a variety ofattractive forces.H3NⓇX#3Hcommand80F3ED4| сF4RIdentify the type of interaction depicted here.FL15⁰%VF5TQuestion 13.e of 36G>6MacBook AirBF6YH&7«F7UA) ion-ion bondsB) disulfide bondsC) hydrogen bonding between functionalgroups on amino acid residue side chainsD) hydrogen bonding between the carbonyland NH of the backbone of the proteinE) hydrophobic attractions (London Dispersionforces) between nonpolar amino acid residueside chains8JDIIF8N M9KF90H0F10LBABIPIcommand option3F111?F121}1

Answered: Image /qna-images/answer/4942a571-1965-4d7f-aefc-dfb70823ec76.jpg

Proteins have complex three-dimensional structures. These polymers are held into these specific shapes with a variety of intermolecular forces, covalent bonds, and ionic bonds. Proteins fold into complex tertiary shapes that are held in place with a variety of attractive forces. Identify the type of interaction depicted here. H₂N A) ion-ion bonds B) disulfide bonds C) hydrogen bonding between functional groups on amino acid residue side chains D) hydrogen bonding between the carbonyl and NH of the backbone of the protein E) hydrophobic attractions (London Dispersion forces) between nonpolar amino acid residue side chains

Proteins have complex three-dimensional structures. These polymers are held into these specific shapes with a variety of intermolecular forces, covalent bonds, and ionic bonds. Proteins fold into complex tertiary shapes that are held in place with a variety of attractive forces. Identify the type of interaction depicted here. H₂N A) ion-ion bonds B) disulfide bonds C) hydrogen bonding between functional groups on amino acid residue side chains D) hydrogen bonding between the carbonyl and NH of the backbone of the protein E) hydrophobic attractions (London Dispersion forces) between nonpolar amino acid residue side chains

Chemistry: The Molecular Science

5th Edition

ISBN:9781285199047

Author:John W. Moore, Conrad L. Stanitski

Publisher:John W. Moore, Conrad L. Stanitski

Chapter10: Fuels, Organic Chemicals, And Polymers

Section10.7: Biopolymers: Polysaccharides And Proteins

Problem 10.20CE

See similar textbooks

Similar questions

Why are the predominant IMFs in CH3(CH2)8OH dispersion forces and not hydrogen bonding?
The structure shown is an example of a type of macromolecule (carbohydrate, lipid, protein, or nucleic acid) that is an important biological polymer. Identify the type of macromolecule shown, the type of monomer it is made from, how you came to your conclusion and the general types of important biological functions of this type of macromolecule in the cell. 0=210 + OCH₂ NH₂ OH OH
A long polymer chain, such as polyethylene ( -CH2CH2- )n, can potentially exist in solution as a chiral object. Give two examples of chiral structures that a polyethylene chain could adopt.
10. Draw the structure of the polymer Glu-Thr-Met-Tyr-Lys. What type of compound is this polymer? What is the functional group that connects the units of this polymer together? Identify it in your drawing. Identify one type of 3° structure interaction in this polymer and illustrate it in your drawing.
PTFE polymer has a very high crystallinity among known commercial polymers. write down the reasons
Which classes of amino acids have side chains that can form ion-dipole interactions with water?
(b) Polymers play essential and ubiquitous roles in our everyday life because of their broad spectrum of properties. (i) List TWO (2) polymers that you encounter everyday. (ii) Describe the properties of each polymer in (i).
Which of the following amino acids have R groups that have hydrogen-bonding potential? Explain. Ala, Gly, Ser, Phe, Glu, Tyr, Ile, and Thr
Intramolecular forces of attraction are often important in holding large molecules together. For example, some proteins fold into compact shapes, held together by attractive forces between nearby functional groups. A schematic of a folded protein is drawn here, with the protein backbone indicated by a blue-green ribbon, and various appendages drawn dangling from the chain. What types of intramolecular forces occur at each labeled site (A–F)?
13. Explain the relationship between chain symmetry and density of polymers.
It's unclear to me what the word "homogeneous structure" really refers to.
Intramolecular forces of attraction are often important in holding largemolecules together. For example, some proteins fold into compactshapes, held together by attractive forces between nearby functionalgroups. A schematic of a folded protein is drawn here, with the proteinbackbone indicated by a blue-green ribbon, and various appendagesdrawn dangling from the chain. What types of intramolecular forcesoccur at each labeled site (A–F)?