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CB > 1 , 4 > Flashcards

1 , 4 Flashcards

1
Q

What is the common genetic flow process found in all living cells?

A

DNA → RNA → Protein

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2
Q

n what form is genetic information stored in all living organisms?

A

DNA

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3
Q

T/F: Viruses are considered living organisms

A

False

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4
Q

How do viruses reproduce if they are not considered living?

A

They use the host cell’s machinery to replicate

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5
Q

What are proteins made of?

A

Proteins are made of 20 different types of amino acids

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6
Q

T/F: Amino acids are linked by hydrogen bonds in a polypeptide

A

False: Amino acids are linked by covalent peptide bonds

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7
Q

What is essential for the folding of proteins?

A

Peptide Backbone Hydrogen Bonds

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8
Q

What are the two types of secondary protein structures?

A

alpha helix & beta pleated sheet

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9
Q

α-Helix are formed by ______ bonding between every ___ amino acid

A

hydrogen ; 4th

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10
Q

How are β-pleated sheets formed?

A

By hydrogen bonding between different areas of the polypeptide backbone, forming a zig-zag structure

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11
Q

What is tertiary protein structure?

A

The full 3D shape of a protein, including α-helices, β-sheets, and random coils

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12
Q

Tertiary structure only involves α-helices

A

False. It involves α-helices, β-sheets, and other elements

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13
Q

Which structure determines the functional domains in a protein

A

Tertiary structure

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14
Q

What is the quaternary structure of a protein?

A

The association of multiple polypeptide chains to form a functional protein

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15
Q

T/F: All proteins have quaternary structure

A

False. Only proteins with more than one polypeptide chain have quaternary structure

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16
Q

Give an example of a protein with quaternary structure

A

Hemoglobin

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17
Q

Why is protein folding important?

A

Proper folding is crucial for protein function, and misfolding can lead to diseases

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18
Q

Misfolded proteins cause diseases like….

A

Cystic Fibrosis and Alzheimer’s

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19
Q

T/F: The 3D structure of a protein does not affect its function

A

False. Protein function is directly related to its 3D structure

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20
Q

What determines a protein’s final structure?

A

The amino acid sequence

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21
Q

What kind of bonds hold a ligand in a protein’s binding site?

A

Non-covalent bonds
(hydrogen bonds, electrostatic attractions, van der Waals forces)

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22
Q

T/F: Protein-ligand binding is random

A

False; it is highly specific

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23
Q

What is the function of an enzyme?

A

Enzymes catalyze reactions by lowering the activation energy

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24
Q

T/F: Most drugs inhibit enzymes by blocking the active site.

A

True

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25
Q

What type of enzyme is lysozyme?

A

An enzyme that breaks down bacterial cell walls

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26
Q

What is an allosteric enzyme?

A

An enzyme with multiple binding sites that influence each other

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27
Q

T/F: Phosphorylation always activates a protein

A

False. Phosphorylation can either activate or deactivate a protein

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28
Q

GTP-binding proteins act as…

A

On-off switches
(GTP = ON, GDP = OFF)

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29
Q

What powers motor proteins like myosin and actin?

A

ATP hydrolysis

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30
Q

T/F: Motor proteins move bidirectionally

A

False; Motor proteins move unidirectionally due to irreversible steps

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31
Q

What is the sequence from non-living to living structures in organisms?

A

Atoms → molecules → organelles → cells → tissues → living organisms

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32
Q

T/F: Cells can only grow and reproduce, but they cannot respond to environmental changes

A

False; Cells can also respond to environmental changes

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33
Q

What type of reaction forms a peptide bond between amino acids?

A

A condensation reaction

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34
Q

T/F: Small changes in amino acid sequence, such as in Sickle Cell Disease, can significantly affect protein function

A

True

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35
Q

What advantage does quaternary structure provide to proteins

A

It allows for the construction of large, complex proteins with cooperative functional properties

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36
Q

How does lysozyme lower the activation energy of the reaction?

A

Lysozyme creates a microenvironment where the polysaccharide chain is distorted, weakening its bonds and facilitating hydrolysis

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37
Q

Name a protein that relies on a tightly bound metal atom for its function

A

Hemoglobin, which has an iron atom bound to oxygen in each heme group

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38
Q

T/F: Phosphorylation is a reversible mechanism used to control protein activity

A

True

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39
Q

What does “allosteric” mean in the context of proteins?

A

“Allosteric” means “other shape,” referring to a protein having multiple binding sites that influence each other

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40
Q

What causes the symptoms of viral infections like a cold sore?

A

The symptoms are caused by the lysis (breaking open) of cells, as seen in herpes simplex virus infections

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41
Q

What is lysis?

A

the breakdown of a cell by rupture of the cell wall or membrane

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42
Q

T/F: Higher organisms are made up of a community of cells derived from multiple founder cells

A

False; Higher organisms are made of communities of cells derived from the division of a single founder cell

43
Q

How do cells convert energy?

A

Cells convert energy from one form to another through processes like cellular respiration in mitochondria

44
Q

According to the cell theory, how did cells first arise?

A

Living cells are formed by the division of pre-existing cells

45
Q

Prokaryotic cells have a nucleus while eukaryotic cells do not

A

False; Prokaryotic cells lack a nucleus, while eukaryotic cells have a defined nucleus

46
Q

Name two key differences between prokaryotic and eukaryotic cells

A
  1. Prokaryotic cells lack membrane-bound organelles, while eukaryotic cells contain membrane-bound organelles
  2. Prokaryotic cells are generally smaller in size, while eukaryotic cells are larger.
47
Q

Which of the following is not a feature of prokaryotic cells?

A) Single, circular DNA molecule
B) Ribosomes
C) Mitochondria

A

C) Mitochondria

48
Q

What is an example of a prokaryotic organism?

A

Bacteria

49
Q

T/F: Eukaryotic cells are typically found in animals, plants, and fungi

A

True

50
Q

Which type of cells undergo mitosis?

A

Eurkaryotic

51
Q

What is the main function of the nucleus in eukaryotic cells?

A

The nucleus stores and protects the cell’s genetic material (DNA) and coordinates cell activities like growth and reproduction

52
Q

T/F: The mitochondria are responsible for protein synthesis

A

False; The mitochondria are responsible for energy production (ATP), while ribosomes are responsible for protein synthesis.

53
Q

What is the function of the endoplasmic reticulum (ER)?

A

The ER functions in the synthesis of proteins (rough ER) and lipids (smooth ER)

54
Q

The Golgi apparatus is primarily responsible for:

A) Breaking down cellular waste
B) Modifying, sorting, and packaging proteins and lipids
C) Synthesizing carbohydrates

A

B) Modifying, sorting, and packaging proteins and lipids

55
Q

What is the primary function of the ribosomes?

A

Protein Synthesis

56
Q

T/F: Chloroplasts are found in animal cells

A

False; Chloroplasts are found in plant cells

57
Q

Chloroplasts are responsible for…

A

photosynthesis

58
Q

What is the role of the cytoskeleton in a cell?

A

The cytoskeleton provides structural support, aids in cell movement, and helps in the organization of the cell’s components

59
Q

Which organelle is known as the “powerhouse of the cell”?

A

The mitochondrion, because it produces energy in the form of ATP

60
Q

Do prokaryotic cells have internal membrane-bound organelles?

A

No, prokaryotic cells do not have internal membrane-bound organelles

61
Q

What is the main method of reproduction in prokaryotic cells?

A) Binary fission
B) Mitosis
C) Meiosis

A

A) Binary Fission

62
Q

Name two organelles that are unique to plant cell

A

Chloroplasts and the cell wall

63
Q

T/F: Both plant and animal cells contain a cell wall

A

False; only plant cells do

64
Q

In which organelle does photosynthesis occur?

A

Chloroplast

65
Q

Define “cytoplasm”

A

Cytoplasm is the gel-like substance within the cell membrane that contains organelles and the cytoskeleton

66
Q

T/F: The plasma membrane is involved in regulating what enters and leaves the cell

A

True

67
Q

What is the function of lysosomes in eukaryotic cells?

A

Lysosomes break down waste materials and cellular debris using enzymes

68
Q

What structure controls the movement of substances in and out of the cell?

A

Plasma Membrane

69
Q

What is the primary structure of a protein?

A

The sequence of amino acids in a polypeptide chain

70
Q

How is the primary structure of a protein held together?

A

By covalent peptide bonds between amino acids

71
Q

What is the secondary structure of a protein?

A

The local folding of the polypeptide chain into structures such as α-helices and β-pleated sheets

72
Q

What type of bonds are involved in maintaining the secondary structure of proteins?

A

Hydrogen bonds between the backbone atoms of the polypeptide chain

73
Q

Describe the α-helix

A

The α-helix is a spiral structure where the polypeptide chain twists, with hydrogen bonds forming between every fourth amino acid

74
Q

What is the β-pleated sheet?

A

A folded, zig-zag pattern formed by hydrogen bonds between different segments of the polypeptide chain

75
Q

What is the tertiary structure of a protein?

A

The full three-dimensional shape of a protein, including interactions between side chains (R groups) of the amino acids

76
Q

Name at least two interactions that stabilize the tertiary structure of a protein

A

Hydrophobic interactions, hydrogen bonds, ionic bonds, and disulfide bridges

77
Q

What is the quaternary structure of a protein?

A

The association of multiple polypeptide chains (subunits) into a functional protein complex

78
Q

Give an example of a protein that has quaternary structure

A

Hemoglobin, which consists of four polypeptide subunits

79
Q

What is the key difference between tertiary and quaternary structures?

A

Tertiary structure refers to the 3D shape of a single polypeptide, while quaternary structure refers to the assembly of multiple polypeptides into a complex

80
Q

What is a protein complex?

A

A structure formed by multiple protein molecules (polypeptides) that interact and function together

81
Q

How do proteins function in complexes within cells?

A

Proteins in complexes often work together to carry out complex functions such as DNA replication, cell signaling, or enzyme activity

82
Q

What advantage does a protein complex have over individual proteins?

A

Protein complexes allow for cooperative interactions, greater regulation, and the ability to perform more complex tasks

83
Q

What is an example of a protein complex in cells?

A

The ribosome, which is a complex of RNA and proteins that synthesizes proteins in the cell

84
Q

Describe how hemoglobin functions as a protein complex

A

Hemoglobin is a complex of four polypeptide subunits, each capable of binding oxygen, allowing the cooperative transport of oxygen in the bloodstream

85
Q

What is a ligand in the context of protein function?

A

A ligand is any molecule that binds specifically to a protein at a binding site

86
Q

What types of bonds are involved in protein-ligand binding?

A

Non-covalent bonds, including hydrogen bonds, electrostatic attractions, and van der Waals forces

87
Q

Where does a ligand bind on a protein?

A

A ligand binds to a specific binding site on the protein

88
Q

What determines the selectivity of protein-ligand binding?

A

The shape and chemical properties of the binding site, which match the ligand like a “lock and key”

89
Q

How do proteins achieve specificity when binding to other molecules?

A

Specificity is achieved by the precise fit between the ligand and the protein’s binding site, requiring many weak bonds to form simultaneously

90
Q

What is the function of an antibody?

A

Antibodies bind to specific foreign molecules (antigens) and help neutralize or eliminate them from the body

91
Q

How many binding sites does an antibody have?

A

An antibody typically has two binding sites, one on each arm of its Y-shaped structure

92
Q

What makes the binding sites of antibodies versatile?

A

The variable regions of antibodies can be altered to bind specifically to a vast range of antigens

93
Q

What part of the antibody is responsible for recognizing antigens?

A

The variable regions at the tips of the antibody arms are responsible for antigen recognition

94
Q

What is the main role of enzymes in the cell?

A

Enzymes act as catalysts that speed up biochemical reactions by lowering the activation energy required for the reaction

95
Q

What is a substrate in enzyme activity?

A

A substrate is the molecule upon which an enzyme acts, binding to the enzyme’s active site

96
Q

How do enzymes lower the activation energy of a reaction?

A

Enzymes create a favorable environment for the reaction by positioning the substrate in a way that facilitates bond-breaking or bond-forming processes

97
Q

What is the active site of an enzyme?

A

The active site is the specific region of the enzyme where the substrate binds and the reaction occurs

98
Q

What is an example of an enzyme and its function?

A

Lysozyme, which breaks down bacterial cell walls by cleaving the bonds in polysaccharides

99
Q

What is allosteric regulation in proteins?

A

Allosteric regulation is when a protein’s function at one site is affected by the binding of a regulatory molecule at a different site

100
Q

What is the role of phosphorylation in protein regulation?

A

Phosphorylation is the addition of a phosphate group to a protein, which can trigger a conformational change that either activates or inactivates the protein

101
Q

What are GTP-binding proteins, and how do they work?

A

GTP-binding proteins act as molecular switches; they are active when bound to GTP and inactive when bound to GDP

102
Q

How does feedback inhibition control enzyme activity?

A

In feedback inhibition, the product of a metabolic pathway inhibits an enzyme involved earlier in the pathway, preventing overproduction of the product

103
Q

How does nucleotide hydrolysis control motor proteins?

A

Motor proteins use the energy from ATP hydrolysis to perform large conformational changes that result in movement, such as muscle contraction

103
Q

What is the significance of protein conformational changes?

A

Conformational changes in a protein can alter its activity, allowing it to perform its function, bind to other molecules, or be regulated

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