Protein Structure and Function Quiz

An interaction between non-polar amino acid side chains within a protein, where they cluster together to avoid contact with water. This plays a major role in forming the protein's core and its dimerization.

A weak, short-range interaction that arises from temporary fluctuations in electron density, creating temporary dipoles in atoms. It can involve both polar and non-polar amino acids and helps tightly pack atoms in protein structures.

An interaction between oppositely charged groups on amino acid side chains within a protein. This interaction helps stabilize the protein's overall structure.

Hydrophobic interactions drive the protein to fold in a specific way, while Van der Waals forces reinforce and stabilize this folded structure by ensuring close contact between atoms.

Ionic bonds are a specific type of electrostatic interaction. They involve the attraction between oppositely charged ions.

A type of interaction between two polar molecules, where the partially positive end of one molecule is attracted to the partially negative end of the other.

A bond formed by the oxidation of two cysteine amino acid side chains.

The concept that a protein's specific three-dimensional shape determines its function.

Proteins that catalyze (speed up) chemical reactions by providing a specific active site where substrates bind.

Fibrous proteins that provide support and shape to cells and tissues.

In sickle cell anemia, the mutation in the hemoglobin gene leads to the replacement of glutamic acid with valine at a specific position in the beta-globin chain.

The triple helix structure of collagen provides tensile strength, enabling it to resist stretching and maintain tissue integrity.

The impact of a mutation in the β-globin gene on hemoglobin is mainly the alteration in its ability to carry oxygen.

Amyloid β peptide aggregates are associated with neurodegenerative diseases, including Alzheimer's disease.

The deposition of amyloid β peptide aggregates contributes to the development of neurodegenerative diseases.

The binding of oxygen to hemoglobin, where the attachment of one oxygen molecule increases the affinity for subsequent oxygen molecules.

When one oxygen (O2) molecule binds to deoxyhemoglobin, it causes a structural change in the hemoglobin molecule. This makes it easier for the remaining heme groups to bind O2.

The allosteric property of hemoglobin is a result of the arrangement of its four subunits, which can interact with each other during oxygen binding. This arrangement is known as the quaternary structure.

The incorrect folding of a protein, which can occur spontaneously or due to genetic mutations.

A group of diseases caused by the buildup of misfolded proteins, called amyloid fibrils, which can damage organs and tissues.

A peptide that is part of the amyloid precursor protein. When it misfolds and aggregates, it forms amyloid plaques in the brain, which are associated with Alzheimer's disease.

A protein that can misfold into a Scrapie form, leading to the formation of amyloid-like fibrils. This can cause neurodegenerative diseases through a process called protein templating.

A change in the DNA sequence that can affect the structure and function of hemoglobin. This can lead to various hemoglobinopathies, such as sickle cell disease and thalassemia.

The linear sequence of amino acids in a polypeptide chain. It's like the alphabet of a protein, determining its basic building blocks.

Three-dimensional folding of a single polypeptide chain. It's like the shape a folded piece of paper takes.

The arrangement of multiple polypeptide chains in a protein. It's like multiple folded pieces of paper interacting with each other.

The process of a protein losing its three-dimensional structure, disrupting its biological function. It's like unfolding a folded piece of paper.

The most common configuration of peptide bonds found in proteins. It's like two beads connected in a straight line, not a bend.

A type of protein misfolding disease characterized by the accumulation of misfolded amyloid-beta plaques in the brain. It can lead to cognitive decline and memory loss.

The amino acid proline is known to disrupt alpha-helices in proteins. It acts as a 'helix breaker'.

A change in a single amino acid in a protein's sequence can disrupt its alpha-helical structure. It's like changing one letter in a word, affecting its meaning.

These bonds play a crucial role in stabilizing the secondary, tertiary, and quaternary structures of proteins. They are also vital in the formation of the active site of enzymes.

This structure is formed through hydrogen bonding interactions between the backbone atoms of the polypeptide chain. It includes the α-helix (coiled) and β-sheet (folded) structures.