교과서 질문
How do the following interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could give rise to each interaction.
b. Disulfide bonds
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Ch.18 Amino Acids and Proteins
McMurry8th EditionFundamentals of General, Organic, and Biological ChemistryISBN: 9780134015187
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TOC.tableOfContents
- Ch.1 Matter and Measurements27
- Ch.2 Atoms and the Periodic Table20
- Ch.3 Ionic Compounds8
- Ch.4 Molecular Compounds23
- Ch.5 Classification & Balancing of Chemical Reactions12
- Ch.6 Chemical Reactions: Mole and Mass Relationships28
- Ch.7 Chemical Reactions: Energy, Rate and Equilibrium64
- Ch.8 Gases, Liquids and Solids24
- Ch.9 Solutions52
- Ch.10 Acids and Bases25
- Ch.11 Nuclear Chemistry22
- Ch.12 Introduction to Organic Chemistry: Alkanes57
- Ch.13 Alkenes, Alkynes, and Aromatic Compounds47
- Ch.14 Some Compounds with Oxygen, Sulfur, or a Halogen50
- Ch.15 Aldehydes and Ketones45
- Ch.16 Amines42
- Ch.17 Carboxylic Acids and Their Derivatives57
- Ch.18 Amino Acids and Proteins82
- Ch.19 Enzymes and Vitamins63
- Ch.20 Carbohydrates44
- Ch.21 The Generation of Biochemical Energy65
- Ch.22 Carbohydrate Metabolism45
- Ch.23 Lipids42
- Ch.24 Lipid Metabolism33
- Ch.25 Protein and Amino Acid Metabolism24
- Ch.26 Nucleic Acids and Protein Synthesis45
McMurry8th EditionFundamentals of General, Organic, and Biological ChemistryISBN: 9780134015187당신이 사용하는 게 아니라요?교과서 변경
18장, 문제 86a
How do the following noncovalent interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could give rise to each interaction.
a. Hydrophobic interactions
검증된 단계별 안내1
Understand the concept of hydrophobic interactions: These occur when nonpolar (hydrophobic) side chains of amino acids cluster together to avoid contact with water. This minimizes the disruption of hydrogen bonding in the surrounding aqueous environment, stabilizing the protein structure.
Recognize the role of hydrophobic interactions in protein folding: In the tertiary structure, hydrophobic side chains are typically buried in the interior of the protein, away from water, while hydrophilic side chains are exposed on the surface. This arrangement contributes to the overall stability of the protein.
Identify amino acids with nonpolar side chains: Examples of amino acids that participate in hydrophobic interactions include leucine, isoleucine, valine, phenylalanine, and alanine. These amino acids have side chains that are nonpolar and hydrophobic.
Provide an example of a pair of amino acids: A pair such as leucine and valine could interact through hydrophobic interactions. Their nonpolar side chains would cluster together in the protein's interior to avoid water.
Relate hydrophobic interactions to protein structure: These interactions help stabilize the tertiary structure by driving the folding process, ensuring that the protein adopts a functional three-dimensional shape. In quaternary structures, hydrophobic interactions can also stabilize the association between different protein subunits.
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주요 개념
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Hydrophobic Interactions
Hydrophobic interactions occur when nonpolar amino acids aggregate to avoid contact with water, which stabilizes protein structures. This phenomenon is crucial in the folding of proteins, as it drives the formation of a hydrophobic core, minimizing the exposure of hydrophobic side chains to the aqueous environment. An example of amino acids involved in this interaction is phenylalanine and leucine.
추천 영상:
가이드 코스
2:41
Interactions within the Tertiary Structure Concept 2
Tertiary Structure
The tertiary structure of a protein refers to its three-dimensional shape formed by the folding of the polypeptide chain. This structure is stabilized by various interactions, including hydrophobic interactions, hydrogen bonds, ionic bonds, and disulfide bridges. The specific arrangement of amino acids in the tertiary structure is critical for the protein's functionality.
추천 영상:
가이드 코스
2:07Tertiary Protein Structure Concept 1
Quaternary Structure
Quaternary structure refers to the assembly of multiple polypeptide chains into a single functional protein complex. This structure is stabilized by noncovalent interactions, such as hydrophobic interactions and hydrogen bonds, between the different subunits. An example of quaternary structure is hemoglobin, which consists of four polypeptide chains that work together to transport oxygen.
추천 영상:
가이드 코스
3:26Quaternary Protein Structure Concept 1
관련 실천
교과서 질문
Give an example of a protein that has quaternary structure. How many polypeptide chains are present in this protein?
758
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교과서 질문
Explain how a protein is denatured by the following:
a. Heat
교과서 질문
What is meant by the following terms as they apply to protein structure, and what bonds or molecular interactions stabilize that level of structure?
d. Quaternary structure
721
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교과서 질문
What level of protein structure is determined by the following:
a. Peptide bonds between amino acids?
1051
views
교과서 질문
What level of protein structure is determined by the following:
b. Hydrogen bonds between backbone carbonyl oxygen atoms and hydrogen atoms attached to backbone nitrogen atoms?
826
views