Textbook Question
Most proteins are soluble in the aqueous environment of a cell. Knowing that, where in the overall three-dimensional shape of a protein would you expect to find amino acids with hydrophobic R groups?
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Ch. 3 The Molecules of Cells
Taylor, Simon, Dickey, Hogan10th EditionCampbell Biology: Concepts & ConnectionsISBN: 9780136538783
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Table of contents
- Ch. 1 Biology: The Study of Scientific Life19
- Ch. 2 The Chemical Basis of Life17
- Ch. 3 The Molecules of Cells21
- Ch. 4 A Tour of the Cell20
- Ch. 5 The Working Cell17
- Ch. 6 How Cells Harvest Chemical Energy18
- Ch. 7 Photosynthesis: Using Light to Make Food15
- Ch. 8 The Cellular Basis of Reproduction and Inheritance22
- Ch. 9 Patterns of Inheritance17
- Ch. 10 Molecular Biology of the Gene13
- Ch. 11 How Genes Are Controlled13
- Ch. 12 DNA Technology and Genomics23
- Ch. 13 How Populations Evolve17
- Ch. 14 The Origin of Species19
- Ch. 15 Tracing Evolutionary History18
- Ch. 16 Microbial Life: Prokaryotes and Protists16
- Ch. 17 The Evolution of Plant and Fungal Diversity15
- Ch. 18 The Evolution of Invertebrate Diversity13
- Ch. 19 The Evolution of Vertebrate Diversity18
- Ch. 20 Unifying Concepts of Animal Structure and Function11
- Ch. 21 Nutrition and Digestion16
- Ch. 22 Gas Exchange16
- Ch. 23 Circulation17
- Ch. 24 The Immune System16
- Ch. 25 Control of Body Temperature and Water Balance20
- Ch. 26 Hormones and the Endocrine System10
- Ch. 27 Reproduction and Embryonic Development12
- Ch. 28 Nervous Systems10
- Ch. 29 The Senses12
- Ch. 30 How Animals Move19
- Ch. 31 Plant Structure, Growth, and Reproduction9
- Ch. 32 Plant Nutrition and Transport12
- Ch. 33 Control Systems in Plants15
- Ch. 34 The Biosphere: An Introduction to Earth's Diverse Environments15
- Ch. 35 Behavioral Adaptations to the Environment12
- Ch. 36 Population Ecology15
- Ch. 37 Communities and Ecosystems14
- Ch. 38 Conservation Biology14
Taylor, Simon, Dickey, Hogan10th EditionCampbell Biology: Concepts & ConnectionsISBN: 9780136538783Not the one you use?Change textbook
Chapter 3, Problem 14
What are the two types of secondary structures found in polypeptides, and what maintains them?
What stabilizes the tertiary structure of a polypeptide?
Verified step by step guidance1
The two types of secondary structures found in polypeptides are the alpha-helix (α-helix) and the beta-pleated sheet (β-sheet). These structures are formed by the folding of the polypeptide chain in specific patterns.
The secondary structures are maintained by hydrogen bonds. In the α-helix, hydrogen bonds form between the carbonyl oxygen (C=O) of one amino acid and the amide hydrogen (N-H) of another amino acid four residues away. In the β-sheet, hydrogen bonds form between the carbonyl oxygen and amide hydrogen of amino acids in adjacent strands.
The tertiary structure of a polypeptide refers to its three-dimensional shape, which is formed by the folding and interactions of the secondary structures.
The tertiary structure is stabilized by various interactions, including hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges. Disulfide bridges are covalent bonds formed between the sulfur atoms of two cysteine residues.
These interactions collectively contribute to the overall stability and functionality of the protein, allowing it to perform its biological role effectively.
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Key Concepts
Here are the essential concepts you must grasp in order to answer the question correctly.
Secondary Structure of Proteins
The secondary structure of proteins refers to the local folded structures that form within a polypeptide due to hydrogen bonding between the backbone atoms. The two most common types are alpha helices, which are coiled structures, and beta sheets, which are flat, sheet-like arrangements. These structures are crucial for the overall shape and function of proteins.
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Hydrogen Bonds
Hydrogen bonds are weak interactions that occur between a hydrogen atom covalently bonded to an electronegative atom and another electronegative atom. In the context of protein secondary structures, these bonds stabilize the alpha helices and beta sheets by forming between the carbonyl oxygen of one amino acid and the amide hydrogen of another. This interaction is essential for maintaining the integrity of the protein's structure.
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Tertiary Structure of Proteins
The tertiary structure of a protein is its overall three-dimensional shape, formed by the interactions between the side chains of the amino acids. This structure is stabilized by various forces, including hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges. The tertiary structure is critical for the protein's functionality, as it determines how the protein interacts with other molecules.
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Related Practice
Textbook Question
Sucrose is broken down in your intestine to the monosaccharides glucose and fructose, which are then absorbed into your blood. What is the name of this type of reaction?
Using this diagram of sucrose, show how this would occur.
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Textbook Question
Explain the role of complementary base pairing in the functions of nucleic acids.
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Textbook Question
The diversity of life is staggering. Yet the molecular logic of life is simple and elegant: small molecules common to all organisms are ordered into unique macromolecules. Explain why carbon is central to this diversity of organic molecules.
How do carbon skeletons, chemical groups, monomers, and polymers relate to this molecular logic of life?
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Textbook Question
How can a cell make many different kinds of proteins out of only 20 amino acids?
Of the myriad possibilities, how does the cell 'know' which proteins to make?
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Textbook Question
Given that the function of egg yolk is to nourish and support the developing chick, explain why egg yolks are so high in fat, protein, and cholesterol.
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