IDK

Question 1

What are enzymes?

Answer 1

Enzymes are biological catalysts that speed up chemical reactions in living organisms.

Question 2

True or False: All enzymes are proteins.

Answer 2

False. Some enzymes are RNA molecules, known as ribozymes.

Question 3

What is the active site of an enzyme?

Answer 3

The active site is the region on the enzyme where substrate molecules bind and undergo a chemical reaction.

Question 4

Fill in the blank: Enzymes lower the ________ energy of a reaction.

Answer 4

activation

Question 5

What is a substrate?

Answer 5

A substrate is the reactant molecule upon which an enzyme acts.

Question 6

What is enzyme specificity?

Answer 6

Enzyme specificity refers to the ability of an enzyme to select and catalyze only one specific substrate or a group of closely related substrates.

Question 7

What are inhibitors?

Answer 7

Inhibitors are molecules that decrease or prevent enzyme activity.

Question 8

True or False: Competitive inhibitors bind to the active site of an enzyme.

Answer 8

True.

Question 9

What is the difference between competitive and non-competitive inhibitors?

Answer 9

Competitive inhibitors bind to the active site, while non-competitive inhibitors bind to a different site on the enzyme, reducing its activity regardless of substrate concentration.

Question 10

What is allosteric regulation?

Answer 10

Allosteric regulation is the process by which an enzyme’s activity is regulated by the binding of an effector molecule at a site other than the active site.

Question 11

Fill in the blank: The primary structure of a protein refers to its ________ sequence.

Answer 11

amino acid

Question 12

What are the four levels of protein structure?

Answer 12

The four levels of protein structure are primary, secondary, tertiary, and quaternary.

Question 13

Short answer: What is the secondary structure of proteins?

Answer 13

The secondary structure refers to the local folded structures that form within a protein due to hydrogen bonding, commonly in the form of alpha helices and beta sheets.

Question 14

True or False: Tertiary structure is the overall 3D shape of a protein.

Answer 14

True.

Question 15

What stabilizes the tertiary structure of a protein?

Answer 15

The tertiary structure is stabilized by various interactions, including hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges.

Question 16

What is quaternary structure?

Answer 16

Quaternary structure refers to the assembly of multiple polypeptide chains into a single functional protein complex.

Question 17

Fill in the blank: Amino acids are linked together by ________ bonds.

Answer 17

peptide

Question 18

What are the essential amino acids?

Answer 18

Essential amino acids are those that cannot be synthesized by the body and must be obtained from the diet.

Question 19

True or False: There are 20 standard amino acids.

Answer 19

True.

Question 20

What role do enzymes play in metabolism?

Answer 20

Enzymes facilitate metabolic reactions by lowering the activation energy required for the reaction to proceed.

Question 21

What is enzyme kinetics?

Answer 21

Enzyme kinetics is the study of the rates of enzyme-catalyzed reactions.

Question 22

What is the Michaelis-Menten equation used for?

Answer 22

The Michaelis-Menten equation describes the rate of enzymatic reactions with respect to substrate concentration.

Question 23

Short answer: What does Vmax represent in enzyme kinetics?

Answer 23

Vmax represents the maximum rate of reaction when the enzyme is saturated with substrate.

Question 24

What is Km in enzyme kinetics?

Answer 24

Km is the Michaelis constant, representing the substrate concentration at which the reaction rate is half of Vmax.

Question 25

Fill in the blank: Proteins are made up of ________.

Answer 25

amino acids

Question 26

What determines the unique properties of each amino acid?

Answer 26

The unique properties of each amino acid are determined by its side chain (R group).

Question 27

What is a disulfide bridge?

Answer 27

A disulfide bridge is a covalent bond formed between the sulfur atoms of two cysteine residues in a protein, contributing to its stability.

Question 28

True or False: Peptide bonds are formed through hydrolysis.

Answer 28

False. Peptide bonds are formed through dehydration synthesis.

Question 29

What is the role of chaperone proteins?

Answer 29

Chaperone proteins assist in the proper folding of other proteins, preventing misfolding and aggregation.

Question 30

What is denaturation in proteins?

Answer 30

Denaturation is the process where a protein loses its native structure due to external stress, such as heat or pH changes.

Question 31

Fill in the blank: The pH at which an amino acid has no net charge is called its ________ point.

Answer 31

isoelectric

Question 32

What are the three components of an amino acid?

Answer 32

An amino group, a carboxyl group, and a side chain (R group).

Question 33

What is a cofactor?

Answer 33

A cofactor is a non-protein molecule that assists in enzyme activity, which can be a metal ion or an organic molecule (coenzyme).

Question 34

True or False: Enzymes can be reused after a reaction.

Answer 34

True.

Question 35

What is the significance of the enzyme-substrate complex?

Answer 35

The enzyme-substrate complex is crucial for the catalytic process, allowing substrates to be converted into products.

Question 36

Fill in the blank: The linear sequence of amino acids in a protein is referred to as its ________ structure.

Answer 36

primary

Question 37

What type of bond involves the sharing of electron pairs between atoms?

Answer 37

Covalent bond

Question 38

True or False: Ionic bonds form between atoms with similar electronegativities.

Answer 38

False

Question 39

Fill in the blank: The bond that forms due to the attraction between positively and negatively charged ions is called a __________ bond.

Answer 39

Ionic

Question 40

Which type of bond is primarily responsible for the secondary structure of proteins?

Answer 40

Hydrogen bonds

Question 41

What type of interaction is characterized by the transient attraction between nonpolar molecules?

Answer 41

Van der Waals forces

Question 42

Multiple Choice: Which type of bond is the strongest? A) Hydrogen B) Ionic C) Covalent D) Van der Waals

Answer 42

C) Covalent

Question 43

What type of bond stabilizes the three-dimensional structure of proteins by forming between the side chains of amino acids?

Answer 43

Disulfide bonds

Question 44

True or False: Hydrogen bonds can form between molecules that are not polar.

Answer 44

False

Question 45

Fill in the blank: The bond formed between two cysteine residues in proteins is called a __________ bond.

Answer 45

Disulfide

Question 46

What type of bond is typically involved in the formation of nucleic acids?

Answer 46

Phosphodiester bond

Question 47

Multiple Choice: Which of the following bonds is essential for the double helix structure of DNA? A) Ionic B) Hydrogen C) Covalent D) Disulfide

Answer 47

B) Hydrogen

Question 48

What type of bond is formed when electrons are transferred from one atom to another?

Answer 48

Ionic bond

Question 49

True or False: Van der Waals forces are significant in stabilizing the structure of large biomolecules.

Answer 49

True

Question 50

Fill in the blank: The type of bond that allows for the flexibility and adaptability of proteins is primarily due to __________ bonds.

Answer 50

Hydrogen

Question 51

What type of bond connects the sugar and phosphate groups in DNA?

Answer 51

Phosphodiester bond