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BIO112 > Chapter 10 > Flashcards

Chapter 10 Flashcards

1
Q

What are the building blocks of proteins?

A

Amino acids

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2
Q

How many standard amino acids are there?

A

20

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3
Q

True or False: Amino acids are linked together by peptide bonds to form proteins.

A

True

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4
Q

What is the primary structure of a protein?

A

The linear sequence of amino acids

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5
Q

What is the secondary structure of a protein?

A

Regular, repeated patterns of folding within localized segments of the polypeptide chain

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6
Q

What are the two most common types of secondary structure in proteins?

A

Alpha helix and beta sheet

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7
Q

What is the tertiary structure of a protein?

A

The overall 3D shape of a polypeptide chain

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8
Q

What is the quaternary structure of a protein?

A

The arrangement of multiple polypeptide chains in a protein complex

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9
Q

What is denaturation of a protein?

A

The loss of a protein’s native structure due to heat, pH changes, or other factors

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10
Q

What is the function of chaperone proteins in protein folding?

A

To help other proteins fold correctly and prevent misfolding

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11
Q

What is the difference between an essential and non-essential amino acid?

A

Essential amino acids must be obtained from the diet, while non-essential amino acids can be synthesized by the body

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12
Q

Which amino acid is known as the ‘building block of life’?

A

Alanine

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13
Q

What is the isoelectric point of an amino acid?

A

The pH at which an amino acid carries no net charge

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14
Q

What is the primary function of proteins in the body?

A

To serve as structural components, enzymes, hormones, antibodies, and transport molecules

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15
Q

What is the difference between a zwitterion and a free amino acid?

A

A zwitterion has both a positive and negative charge, while a free amino acid has one charge

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16
Q

What is the significance of the R-group in an amino acid?

A

It determines the specific properties and function of each amino acid

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17
Q

What is the difference between a hydrophobic and hydrophilic amino acid?

A

Hydrophobic amino acids repel water, while hydrophilic amino acids attract water

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18
Q

What is a disulfide bond in protein structure?

A

A covalent bond between two sulfur atoms in two cysteine amino acids

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19
Q

What is the role of proline in protein structure?

A

Proline disrupts the secondary structure due to its unique cyclic structure

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20
Q

What is the significance of the glycosylation of proteins?

A

It plays a role in protein folding, stability, and recognition

21
Q

What is the Ramachandran plot used for in protein structure analysis?

A

To analyze the allowed regions of dihedral angles in a polypeptide chain

22
Q

What is the difference between a globular and fibrous protein structure?

A

Globular proteins are compact and water-soluble, while fibrous proteins are elongated and insoluble

23
Q

What is the significance of the N-terminus and C-terminus in protein structure?

A

They indicate the beginning and end of a polypeptide chain, respectively

24
Q

Which amino acid is commonly found in collagen?

A

Glycine

25
Q

What is the role of histidine in enzyme catalysis?

A

It acts as a general acid-base catalyst in enzyme reactions

26
Q

What is the role of asparagine in protein structure?

A

It is involved in protein folding and stability due to its ability to form hydrogen bonds

27
Q

How does pH affect protein structure?

A

Extreme pH values can disrupt protein folding and denature proteins

28
Q

What is the significance of the hydrophobic effect in protein folding?

A

Hydrophobic amino acids tend to cluster together to minimize contact with water, driving protein folding

29
Q

What is the difference between a primary and quaternary structure of a protein?

A

Primary structure is the linear sequence of amino acids, while quaternary structure involves the arrangement of multiple polypeptide chains

30
Q

What is the role of disulfide bonds in stabilizing protein structure?

A

Disulfide bonds covalently link cysteine residues to form loops or bridges in proteins

31
Q

What is the function of collagen in the body?

A

To provide structural support and strength to tissues like skin, bones, and cartilage

32
Q

What is the structure of an alpha helix in proteins?

A

A right-handed helical structure stabilized by hydrogen bonds between the carbonyl oxygen and amide hydrogen atoms

33
Q

What is the significance of beta turns in protein structure?

A

Beta turns reverse the direction of a polypeptide chain, allowing it to fold back on itself

34
Q

What is the difference between a peptide bond and a disulfide bond in protein structure?

A

Peptide bonds link amino acids in a polypeptide chain, while disulfide bonds covalently link cysteine residues

35
Q

What is the role of a hydrogen bond in protein structure?

A

Hydrogen bonds stabilize secondary structures like alpha helices and beta sheets in proteins

36
Q

What is the difference between a parallel and anti-parallel beta sheet in protein structure?

A

In a parallel beta sheet, adjacent strands run in the same direction, while in an anti-parallel beta sheet, adjacent strands run in opposite directions

37
Q

What is the significance of the Ramachandran plot in protein structure analysis?

A

It shows the allowed regions of dihedral angles in a polypeptide chain, helping to predict protein folding

38
Q

What is the role of hydroxyproline in collagen structure?

A

Hydroxyproline stabilizes the triple helix structure of collagen through hydrogen bonding

39
Q

What is the role of methionine in protein structure?

A

Methionine acts as the starting amino acid in protein synthesis and contains a sulfur atom for disulfide bond formation

40
Q

What is the significance of the quaternary structure in protein function?

A

It allows for the assembly of multiple protein subunits to create functional complexes

41
Q

What is the function of keratin in the body?

A

To provide structural support to hair, nails, and skin

42
Q

What is the role of serine in enzyme catalysis?

A

Serine can act as a nucleophile in enzyme reactions due to its hydroxyl group

43
Q

What is the significance of post-translational modifications in protein structure?

A

They can alter protein function, localization, stability, and activity

44
Q

What is the role of leucine in protein structure?

A

Leucine is commonly found in hydrophobic regions of proteins and plays a role in protein-protein interactions

45
Q

What is the difference between a domain and a motif in protein structure?

A

A domain is a functional unit of a protein with a specific structure and function, while a motif is a smaller structural element with a conserved sequence

46
Q

What is the role of lysine in enzyme catalysis?

A

Lysine can act as a nucleophile in enzyme reactions due to its positively charged amino group

47
Q

What is the significance of the disulfide bond in stabilizing protein structure?

A

Disulfide bonds covalently link cysteine residues to form loops or bridges in proteins

48
Q

What is the difference between a tertiary and quaternary structure in protein organization?

A

Tertiary structure refers to the 3D folding of a single polypeptide chain, while quaternary structure involves the assembly of multiple polypeptide chains

BIO112 (6 decks)

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