Effect of hydrophobic interactions on the tertiary structure of proteins must be explained. Concept introduction: Proteins are biological polymers made up of amino acids. Amino acids are connected through peptide bonds to make polypeptide chains. Amino acids are molecules that contain both amino group and carboxylic acid group attached to the same carbon atom. A peptide bond is formed by condensation of amino group of one amino acid to the carboxylic acid of other amino acid. Structure of proteins plays a very important role in their function. Proteins are very complex in structure. Structure of protein is studied in four levels: Primary, Secondary, Tertiary and Quaternary structure. Primary structure: Primary structure of a protein is the sequence of amino acids in each polypeptide chain that make up the protein. The ultimate structure of protein depends on this sequence. Secondary Structure: The peptide backbone of polypeptide chain folds onto itself due to interactions between amino and carboxylic acid residues in the peptide backbone. This folding of polypeptide chains give proteins a unique shape, this makes the secondary structure of proteins. Two kinds of shapes are formed in the secondary structure of proteins: α-Helix: The backbone folds itself to form a helical structure. Hydrogen bonds are formed with the chain. ß-Pleated sheet: The polypeptide chains are stacked side by side. The outer N-H and C=O form intermolecular hydrogen bonds and give a very rigid structure. These hydrogen bonds are formed between neighboring polypeptide chains unlike α-Helix. Tertiary Structure: The overall 3-Dimensional structure of a protein formed when regions in secondary structure fold together, is called the tertiary structure of a protein. The tertiary structure of a protein is primarily due to interactions between the side chains of the polypeptide chains or the side chains in the backbone of the polypeptide. The interactions between the side chains include: hydrogen bonding, ionic interactions, dipole-dipole interactions and London dispersion forces. Another important interaction that makes up the tertiary structure of proteins are hydrophobic interactions between the hydrophobic r groups of side chain of amino acids. One special kind of covalent bond is also involved in forming the tertiary structure of proteins that is the disulfide bond formed between the -SH residues of cysteine. Quaternary Structure: When proteins contain more than one polypeptide chain, the final arrangement of each polypeptide subunit is known as the quaternary structure. The same kinds of interactions that make the tertiary structure are also involved in forming the quaternary structure.

Question

Br. , H+ .OH Mg ether solvent H+, H₂O 17. Which one of the compounds below is the final product of the reaction sequence shown above? HO A HO HO OH D B OH HO OH C OH HO OH E

Answer 1

Question

Definition Definition Class of organic compounds that contain a carboxyl group ( - COOH ) and has a general formula R - COOH or R - CO 2 H , where R refers to the alkyl, alkenyl, aryl, or other groups. They can undergo different chemical reactions, such as acid-base reactions, esterification, and oxidation. These are essential components of living organisms, playing important roles in metabolic processes, signaling, and as pharmaceuticals.

Chapter 21, Problem 48P

Interpretation Introduction

Interpretation:

Effect of hydrophobic interactions on the tertiary structure of proteins must be explained.

Concept introduction:

Proteins are biological polymers made up of amino acids. Amino acids are connected through peptide bonds to make polypeptide chains.

Amino acids are molecules that contain both amino group and carboxylic acid group attached to the same carbon atom. A peptide bond is formed by condensation of amino group of one amino acid to the carboxylic acid of other amino acid.

Structure of proteins plays a very important role in their function. Proteins are very complex in structure. Structure of protein is studied in four levels: Primary, Secondary, Tertiary and Quaternary structure.

Primary structure:

Primary structure of a protein is the sequence of amino acids in each polypeptide chain that make up the protein. The ultimate structure of protein depends on this sequence.

Secondary Structure:

The peptide backbone of polypeptide chain folds onto itself due to interactions between amino and carboxylic acid residues in the peptide backbone. This folding of polypeptide chains give proteins a unique shape, this makes the secondary structure of proteins.

Two kinds of shapes are formed in the secondary structure of proteins:

α-Helix: The backbone folds itself to form a helical structure. Hydrogen bonds are formed with the chain.

ß-Pleated sheet: The polypeptide chains are stacked side by side. The outer N-H and C=O form intermolecular hydrogen bonds and give a very rigid structure. These hydrogen bonds are formed between neighboring polypeptide chains unlike α-Helix.

Tertiary Structure:

The overall 3-Dimensional structure of a protein formed when regions in secondary structure fold together, is called the tertiary structure of a protein. The tertiary structure of a protein is primarily due to interactions between the side chains of the polypeptide chains or the side chains in the backbone of the polypeptide.

The interactions between the side chains include: hydrogen bonding, ionic interactions, dipole-dipole interactions and London dispersion forces. Another important interaction that makes up the tertiary structure of proteins are hydrophobic interactions between the hydrophobic r groups of side chain of amino acids.

One special kind of covalent bond is also involved in forming the tertiary structure of proteins that is the disulfide bond formed between the -SH residues of cysteine.

Quaternary Structure:

When proteins contain more than one polypeptide chain, the final arrangement of each polypeptide subunit is known as the quaternary structure. The same kinds of interactions that make the tertiary structure are also involved in forming the quaternary structure.

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Br. , H+ .OH Mg ether solvent H+, H₂O 17. Which one of the compounds below is the final product of the reaction sequence shown above? HO A HO HO OH D B OH HO OH C OH HO OH E

8:57 PM Sun Jan 26 Content ← Explanation Page X Content X ALEKS Jade Nicol - Le A https://www-av C www-awa.aleks.com O States of Matter Understanding consequences of important physical properties of liquids ? QUESTION Liquid A is known to have a lower viscosity and lower surface tension than Liquid B. Use these facts to predict the result of each experiment in the table below, if you can. experiment Liquid A and Liquid B are each pumped through tubes with an inside diameter of 27.0 mm, and the pressures PA and PB needed to produce a steady flow of 2.4 mL/s are measured. 25.0 mL of Liquid A are poured into a beaker, and 25.0 mL of Liquid B are poured into an identical beaker. Stirrers in each beaker are connected to motors, and the forces FA and FB needed to stir each liquid at a constant rate are measured. predicted outcome OPA will be greater than PB OPA will be less than PB OPA will be equal to PB It's impossible to predict whether PA or PB will be greater without more information.…

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Answer 2

Question

Definition Definition Class of organic compounds that contain a carboxyl group ( - COOH ) and has a general formula R - COOH or R - CO 2 H , where R refers to the alkyl, alkenyl, aryl, or other groups. They can undergo different chemical reactions, such as acid-base reactions, esterification, and oxidation. These are essential components of living organisms, playing important roles in metabolic processes, signaling, and as pharmaceuticals.

Chapter 21, Problem 48P

Interpretation Introduction

Interpretation:

Effect of hydrophobic interactions on the tertiary structure of proteins must be explained.

Concept introduction:

Proteins are biological polymers made up of amino acids. Amino acids are connected through peptide bonds to make polypeptide chains.

Amino acids are molecules that contain both amino group and carboxylic acid group attached to the same carbon atom. A peptide bond is formed by condensation of amino group of one amino acid to the carboxylic acid of other amino acid.

Structure of proteins plays a very important role in their function. Proteins are very complex in structure. Structure of protein is studied in four levels: Primary, Secondary, Tertiary and Quaternary structure.

Primary structure:

Primary structure of a protein is the sequence of amino acids in each polypeptide chain that make up the protein. The ultimate structure of protein depends on this sequence.

Secondary Structure:

The peptide backbone of polypeptide chain folds onto itself due to interactions between amino and carboxylic acid residues in the peptide backbone. This folding of polypeptide chains give proteins a unique shape, this makes the secondary structure of proteins.

Two kinds of shapes are formed in the secondary structure of proteins:

α-Helix: The backbone folds itself to form a helical structure. Hydrogen bonds are formed with the chain.

ß-Pleated sheet: The polypeptide chains are stacked side by side. The outer N-H and C=O form intermolecular hydrogen bonds and give a very rigid structure. These hydrogen bonds are formed between neighboring polypeptide chains unlike α-Helix.

Tertiary Structure:

The overall 3-Dimensional structure of a protein formed when regions in secondary structure fold together, is called the tertiary structure of a protein. The tertiary structure of a protein is primarily due to interactions between the side chains of the polypeptide chains or the side chains in the backbone of the polypeptide.

The interactions between the side chains include: hydrogen bonding, ionic interactions, dipole-dipole interactions and London dispersion forces. Another important interaction that makes up the tertiary structure of proteins are hydrophobic interactions between the hydrophobic r groups of side chain of amino acids.

One special kind of covalent bond is also involved in forming the tertiary structure of proteins that is the disulfide bond formed between the -SH residues of cysteine.

Quaternary Structure:

When proteins contain more than one polypeptide chain, the final arrangement of each polypeptide subunit is known as the quaternary structure. The same kinds of interactions that make the tertiary structure are also involved in forming the quaternary structure.

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Answer 3

Question

Definition Definition Class of organic compounds that contain a carboxyl group ( - COOH ) and has a general formula R - COOH or R - CO 2 H , where R refers to the alkyl, alkenyl, aryl, or other groups. They can undergo different chemical reactions, such as acid-base reactions, esterification, and oxidation. These are essential components of living organisms, playing important roles in metabolic processes, signaling, and as pharmaceuticals.

Chapter 21, Problem 48P

Interpretation Introduction

Interpretation:

Effect of hydrophobic interactions on the tertiary structure of proteins must be explained.

Concept introduction:

Proteins are biological polymers made up of amino acids. Amino acids are connected through peptide bonds to make polypeptide chains.

Amino acids are molecules that contain both amino group and carboxylic acid group attached to the same carbon atom. A peptide bond is formed by condensation of amino group of one amino acid to the carboxylic acid of other amino acid.

Structure of proteins plays a very important role in their function. Proteins are very complex in structure. Structure of protein is studied in four levels: Primary, Secondary, Tertiary and Quaternary structure.

Primary structure:

Primary structure of a protein is the sequence of amino acids in each polypeptide chain that make up the protein. The ultimate structure of protein depends on this sequence.

Secondary Structure:

The peptide backbone of polypeptide chain folds onto itself due to interactions between amino and carboxylic acid residues in the peptide backbone. This folding of polypeptide chains give proteins a unique shape, this makes the secondary structure of proteins.

Two kinds of shapes are formed in the secondary structure of proteins:

α-Helix: The backbone folds itself to form a helical structure. Hydrogen bonds are formed with the chain.

ß-Pleated sheet: The polypeptide chains are stacked side by side. The outer N-H and C=O form intermolecular hydrogen bonds and give a very rigid structure. These hydrogen bonds are formed between neighboring polypeptide chains unlike α-Helix.

Tertiary Structure:

The overall 3-Dimensional structure of a protein formed when regions in secondary structure fold together, is called the tertiary structure of a protein. The tertiary structure of a protein is primarily due to interactions between the side chains of the polypeptide chains or the side chains in the backbone of the polypeptide.

The interactions between the side chains include: hydrogen bonding, ionic interactions, dipole-dipole interactions and London dispersion forces. Another important interaction that makes up the tertiary structure of proteins are hydrophobic interactions between the hydrophobic r groups of side chain of amino acids.

One special kind of covalent bond is also involved in forming the tertiary structure of proteins that is the disulfide bond formed between the -SH residues of cysteine.

Quaternary Structure:

When proteins contain more than one polypeptide chain, the final arrangement of each polypeptide subunit is known as the quaternary structure. The same kinds of interactions that make the tertiary structure are also involved in forming the quaternary structure.

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Answer 4

Question

Definition Definition Class of organic compounds that contain a carboxyl group ( - COOH ) and has a general formula R - COOH or R - CO 2 H , where R refers to the alkyl, alkenyl, aryl, or other groups. They can undergo different chemical reactions, such as acid-base reactions, esterification, and oxidation. These are essential components of living organisms, playing important roles in metabolic processes, signaling, and as pharmaceuticals.

Chapter 21, Problem 48P

Interpretation Introduction