Biochemistry Chapter 1: Hierarchical Organization

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Questions and Answers

What is the result of differing electronegativities in a molecule?

A complete transfer of electrons

The formation of an electric dipole (correct)

The creation of a triple bond

The breaking of a covalent bond

What is the approximate percentage of oxygen in a human being?

96% (correct)

70%

90%

80%

What is the primary reason for the formation of hydrogen bonds between water molecules?

The similarities in electronegativities between oxygen and hydrogen atoms

The differences in electronegativities between oxygen and hydrogen atoms (correct)

The ability of water to dissolve other polar compounds

The presence of a double bond between oxygen and hydrogen atoms

What is the approximate energy required to break a hydrogen bond?

20 kJ/mol Signup and view all the answers

What is the common trait shared by all living organisms on Earth?

They all have a common origin Signup and view all the answers

How many major types of biomolecules are found in living organisms?

4 Signup and view all the answers

Which of the following functional groups does not form hydrogen bonds?

C-H bonds Signup and view all the answers

What is the number of different amino acids found in biological molecules?

20 Signup and view all the answers

Why do polar compounds dissolve in water?

Because of their ability to form hydrogen bonds with water Signup and view all the answers

What is the variable part of an amino acid?

The R group Signup and view all the answers

What is the term for the electrostatic connections between water molecules?

Hydrogen bonding Signup and view all the answers

What is the result of amino acids polymerizing to form proteins?

A polypeptide chain Signup and view all the answers

What type of interactions are important in biochemistry?

Weak hydrogen bonds Signup and view all the answers

What is the significance of the shape of a protein?

It determines the protein's function Signup and view all the answers

What is the term for the bonding between water and other functional groups?

Hydrogen bonding Signup and view all the answers

What is the name of the force that brings hydrophobic residues together?

Hydrophobic effect Signup and view all the answers

What is the term for the shorter sequence of amino acids that make up a protein?

Peptide Signup and view all the answers

What is the pH of a solution in which the concentration of H+ is equal to the concentration of OH-?

7 Signup and view all the answers

What type of biomolecule is Met-Enkephalin?

A peptide Signup and view all the answers

What is the name of the equation that describes the extent of ionization of water?

Keq Signup and view all the answers

What is the term for the hydrophobic groups in a protein structure?

R groups Signup and view all the answers

What type of bonds are responsible for the stability of protein 3D structure?

All of the above Signup and view all the answers

What is the name of the protein that illustrates the principles of tertiary structure?

Myoglobin Signup and view all the answers

What is the role of proline residues in protein structure?

Initiating bends Signup and view all the answers

What is the term used to describe the clustering of hydrophobic residues in protein structure?

Hydrophobic interactions Signup and view all the answers

What is the term used to describe the process of protein folding into a compact structure?

Tertiary structure Signup and view all the answers

What is a characteristic of proteins that are highly stable?

They are unable to change shape Signup and view all the answers

What is the result of hydrophobic collapse and formation of secondary structures?

A faster formation of 3D structure Signup and view all the answers

What limits the amount of motion a protein can undergo and the number of conformations it can achieve?

The native state of the protein Signup and view all the answers

What is the process of protein folding?

A non-random process Signup and view all the answers

What is the result of the series of smaller changes involving fewer residues?

The acquisition of 3D structure Signup and view all the answers

What is the role of hydrophobic collapse in protein folding?

To speed up the formation of 3D structure Signup and view all the answers

What is true about the free-energy funnel of protein folding?

It is a non-random process Signup and view all the answers

What is the relationship between the number of amino acids and the formation of 3D structure?

There is no relationship between the two Signup and view all the answers

What is the primary function of chaperone proteins in protein folding?

To prevent protein aggregation Signup and view all the answers

What happens to the shape of a chaperone protein when it binds ATP?

It changes shape to bind to misfolded proteins Signup and view all the answers

What is the result of protein misfolding?

Protein aggregation Signup and view all the answers

What is the native structure of a protein?

The final conformation of a protein after synthesis Signup and view all the answers

What is the role of heat shock proteins in protein folding?

To mediate protein folding Signup and view all the answers

What is the result of chaperone proteins releasing misfolded proteins?

The protein folds correctly Signup and view all the answers

What is the characteristic of a protein surface recognized by chaperone proteins?

Hydrophobic surfaces Signup and view all the answers

What are diseases resulting from the formation of protein aggregates called?

Amyloidoses Signup and view all the answers

Study Notes

Hierarchical Organization of a Multicellular Organism

The human body is composed of 96% H, C, N, and O.
Elements in biological molecules vary in their abundance.

Biomolecules

There are 4 major types of biomolecules: amino acids, carbohydrates, lipids, and nucleic acids.
Amino acids are the building blocks of proteins and have a central carbon atom bonded to an amino group, a carboxyl group, and a variable R group.

Amino Acids

There are 20 different amino acids, each with a unique R group.
Amino acids polymerize to form proteins.
Proteins have a primary structure, which is the sequence of amino acids.

Proteins

Proteins have a secondary structure, which is the folding of the polypeptide chain.
Hydrophobic R groups are yellow.
When the polypeptide chain gets long, folding occurs, resulting in a protein.
The shape of a protein is critical to its function.

Hydrogen Bonding

Hydrogen bonds occur between a hydrogen atom in a polar bond and any strongly electronegative atom (usually O or N).
Hydrogen bonds form between alcohols, aldehydes, ketones, and NH groups.
It takes about 20 kJ/mol to break hydrogen bonds.

pH and Biochemistry

pH is an important biochemical parameter.
The extent of ionization is described by Keq.
At 25°C, Keq = 1.8 x 10-16 M.

Protein Structure

Tertiary structure refers to the compact, water-soluble folding of proteins.
Interactions that dictate protein 3D structure include covalent bonds, ionic bonds, hydrogen bonds, Van der Waals forces, and hydrophobic interactions.
Many strong and weak interactions stabilize protein 3D structure.

Myoglobin

Myoglobin illustrates the principles of tertiary structure.
Hydrophobic residues are clustered inside the protein (stabilized by Van der Waals forces).
Hydrophilic residues are on the outside of the protein.

Protein Folding

Protein folding is not a random process.
Hydrophobic collapse and the formation of secondary structure occur rapidly.
A series of smaller changes involving fewer residues leads to the acquisition of 3D structure.

Chaperones

Protein folding is mediated by chaperones.
Chaperones bind to misfolded proteins, preventing them from sticking together.
Chaperones release the protein, allowing it to fold and reach its native state.

Amyloidoses

Amyloidoses are diseases resulting from the formation of protein aggregates, called amyloid fibrils or plaques.

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Description

This quiz covers the basics of biochemistry, focusing on the hierarchical organization of a multicellular organism, particularly the human being. It explores the elements found in biological molecules and their common origin.