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Bio > Biological Molecules > Flashcards

Biological Molecules Flashcards

1
Q

Front: What makes water a polar molecule?

A

Back: Water is polar due to the electronegativity difference between oxygen and hydrogen, leading to unequal sharing of electrons.

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2
Q

Front: What bonds are crucial for water’s properties?

A

Back: Hydrogen bonds are crucial for water’s unique properties.

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3
Q

Front: What causes the dipole moment in water?

A

Back: The unequal sharing of electrons and the partial charges on oxygen (
δ
−
) and hydrogen (
δ
+
) create a dipole moment in water

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4
Q

Front: Why does oxygen attract electrons more strongly than hydrogen?

A

Back: Oxygen is more electronegative than hydrogen, so it attracts electrons more strongly, leading to a partial negative charge on oxygen.

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5
Q

Front: What is the bond angle in a water molecule?

A

Back: The bond angle in a water molecule is approximately 104.5°.

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6
Q

Front: What kind of molecule is water classified as due to its uneven electron distribution?

A

Back: Water is classified as a polar covalent molecule.

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7
Q

Front: What is hydrogen bonding in water?

A

A type of weak bond between the
δ
+
hydrogen atom of one water molecule and the
δ
−
oxygen atom of another water molecule.
Responsible for many unique properties of water.

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8
Q

Front: Why is water considered a universal solvent?

A

Water’s polar nature allows it to dissolve a wide range of substances.
Interacts with polar and charged particles, making it a versatile and essential solvent in biological systems.

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9
Q

Front: What role does water play in biological transport?

A

Facilitates movement of ions, nutrients, and waste within living organisms. Because of
Its ability to dissolve charged molecules

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10
Q

Front: How does water’s dipole nature affect its properties?

A

The dipole nature enables water to form hydrogen bonds.
Contributes to its high surface tension, boiling point, and its capabilities as a solvent.

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11
Q

Front:
Name three common monosaccharides

A

Glucose, Galactose, Fructose

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12
Q

What are two key properties of monosaccharides?

A

Monosaccharides are sweet and soluble in water

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13
Q

What polymers are made up of glucose subunits?

A

Starch and glycogen are polymers made of glucose subunits

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14
Q

What are disaccharides made of

A

Two monosaccharides joined together (e.g., sucrose = glucose + fructose).

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15
Q

How are the two monosaccharides in disaccharides joined

A

They are joined in a condensation reaction, removing a molecule of water.

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16
Q

What type of bond links the two monosaccharides

A

A glycosidic bond.

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17
Q

What is a 1-4 glycosidic bond?

A

It is when carbon 1 of one molecule is attached to carbon 4 of another

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18
Q

How can the glycosidic bond be broken?

A

By hydrolysis, which is the splitting of molecules with the addition of water.

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19
Q

In what process does hydrolysis occur in disaccharides?

A

During digestion in the gut and when stored carbohydrates are broken down to release sugars.

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20
Q

What is a common characteristic of most disaccharides?

A

They are sweet

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21
Q

What is a common characteristic of most disaccharides?

A

They are sweet

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22
Q

Amylopectin Structure

A

Chains linked with α-1,4 glycosidic bonds

Branches with α-1,6 glycosidic bonds every 20-30 monomers

Branched and coiled, compact shape

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23
Q

Amylopectin Function

A

The branching chains have lots of terminal glucose molecule that can be broken off rapidly when energy is needed

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24
Q

Glycogen Structure

A

Composed of α-1,4 and α-1,6 glycosidic bonds
Branches more frequently every 8-12 residues
Forms compact granules for storage

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25
Q

Glycogen Function

A

Primary carbohydrate energy storage in animals
Quickly hydrolyzed for rapid energy release
Regulates glucose concentration levels in cells

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26
Q

Describe the properties of polysaccharides

A

A: Not sweet, difficult to dissolve, and are macromolecules.

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27
Q

Q: What are the components of starch?

A

A: Made of 30% amylose and 70% amylopectin.

28
Q

Describe the structure of amylose

A

Unbranched chains with α-1,4 glycosidic bonds, forming a helical shape

29
Q

How is glucose released from amylose?

A

Enzymes release glucose by working from each end of the amylose molecule

30
Q

What is the primary energy-related function of lipids in animals?

A

They are an important source of energy and energy storage, containing more energy per gram than carbohydrates or proteins

31
Q

Describe the function of lipids in nerve cells.

A

They form a fatty sheath that insulates nerves, helping electrical impulses travel faster.

32
Q

Q: What is the composition of fats and oils?

A

A: Fats and oils are made up of fatty acids and glycerol.

33
Q

Q: What is the chemical formula for glycerol?

A

C₃H₈O₃

34
Q

Q: What are fatty acids made of?

A

A: A long hydrocarbon chain and a carboxylic group (-COOH).

35
Q

Q: What are the two main types of fatty acids?

A

Saturated and unsaturated.

36
Q

Q: Describe the structure of saturated fats.

A

A: They have the maximum number of hydrogen atoms, no double bonds, and long, straight chains.

37
Q

Q: Why are saturated fats solid at room temperature?

A

A: Because their straight chains allow them to pack closely, creating strong intermolecular bonds.

38
Q

What is the chemical structure of stearic acid?

A

CH
3
(
CH
2
)
16
COOH
- A long hydrocarbon chain with a carboxylic acid group.

39
Q

Q: What is formed when a fatty acid joins with a glycerol molecule

A

Mono-, di-, or triglycerides through a process called esterification.

40
Q

What is esterification?

A

A condensation reaction where an ester bond is formed by removing water when a fatty acid reacts with glycerol.

41
Q

Q: What elements do proteins contain?

A

Carbon, hydrogen, oxygen, nitrogen, and sometimes sulfur.

42
Q

How are proteins formed?

A

By condensation reactions between amino acids.

43
Q

What is the basic structure of an amino acid?

A

An amino group (-NH₂), a carboxyl group (-COOH), and a side chain (R group).

44
Q

What type of reaction forms peptide bonds?

A

Condensation reaction.

45
Q

What is the bond formed between amino acids called?

A

A: Peptide link.

46
Q

What does the primary structure of a protein refer to?

A

The sequence of amino acids in its molecules.

47
Q

What is the secondary structure of a protein?

A

The repeating pattern in the structure of peptide chains, such as an alpha helix or beta-pleated sheet, held together by hydrogen bonds.

48
Q

Which bonds are responsible for maintaining the secondary structure of proteins?

A

Hydrogen bonds.

49
Q

What does the tertiary structure of a protein refer to?

A

The three-dimensional (3D) folding of the secondary structure.

50
Q

What types of bonds are involved in stabilizing the tertiary structure of proteins?

A

Hydrogen bonds
Disulfide bonds
Ionic bonds
Van der Waals forces

51
Q

Provide an example of a protein with a quaternary structure and how it’s formed

A

Hemoglobin, consisting of four polypeptide chains held around a non-protein heme group.

52
Q

🌟 Hydrogen Bonds

A

Form between oxgens in carboxyl groups (COOH) and hydrogens in amino groups (NH₂).

Weak individually, strong collectively.

Important for folding and coiling polypeptide chains.

53
Q

🔗 Sulfur Bridges (Disulfide)

A

Form when 2 cysteine or methionine are close together

Result in strong covalent bonds.

Holed polypeptide structure

54
Q

➕➖ Ionic Bonds

A

Occur between positively and negatively charged side chains.
Buried deep in proteins, very strong.

55
Q

🧵 Fibrous Proteins

A

Little tertiary structure; long parallel chains.

Cross-linkages create fibers.

Insoluble in water, extremely tough.

Examples: keratin, collagen, spider webs.

56
Q

🌐 Globular Proteins

A

Complex tertiary and quaternary structures.

Folded into spherical (globular) shapes.

Ionic properties; form colloids in water.

57
Q

What are conjugated proteins?

A

Proteins that join with another molecule called a prosthetic group.

58
Q

What is one function of glycoproteins?

A

Carbohydrates help them to hold on to lots of water, makes them less likely to be broken down by protein-digesting enzymes

59
Q

What is the structural feature of collagen?

A

Collagen has a unique triple-helical structure.

60
Q

What is the basic structural unit of collagen called?

A

A tropocollagen molecule.

61
Q

How many polypeptide chains form a tropocollagen molecule?

A

Three polypeptide chains (alpha chains).

62
Q

What stabilizes the helical structure of collagen?

A

Hydrogen bonds and covalent cross-links such as hydroxylysine and lysine.

63
Q

What is the structural composition of hemoglobin?

A

It is a tetrameric protein with four subunits.

64
Q

What are the globin chains in adult hemoglobin?

A

Two alpha (α) globin chains and two beta (β) globin chains

65
Q

What is the role of iron ions in heme groups?

A

To bind and transport oxygen.

66
Q

What change occurs in hemoglobin when oxygen binds?

A

It undergoes a change from a Tense (T) state to a Relaxed (R) state, increasing oxygen affinity.

67
Q

What change occurs in hemoglobin when oxygen binds?

A

It undergoes a change from a Tense (T) state to a Relaxed (R) state, increasing oxygen affinity.

Bio (6 decks)

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