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Biochemistry Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

As the distance between the nucleus and the electron increases, what occurs?

A

The chemical potential energy also increases.

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2
Q

If the bond angle is 109’5 degrees, has 0 non bonding pairs, what shape is the molecule?

A

Tetrahedral

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3
Q

If the bond angle is 107 and has 1 non bonding pair, what shape is the molecule?

A

Pyramidal

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4
Q

If the bond angle is 104 and had two non bonding pairs, what shape is the molecule ?

A

Bent

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5
Q

If the bond angle is 180 degrees and has 3 non bonding pairs, what shape is the molecule ?

A

Linear

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6
Q

What is molecular polarity dependent on?

A

Shape and bond polarity

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7
Q

Are symmetrical shapes polar or non polar ?

A

Non polar

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8
Q

Asymmetrical shapes are polar or non polar ?

A

Polar

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9
Q

Are intermolecular forces stronger than intramolecular forces ?

A

No, intramolecular forces are stronger.

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10
Q

What are the three types of intermolecular forces?

A

London dispersion forces, dipole-dipole forces and hydrogen bonding .

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11
Q

What is the weakest intermolecular force ?

A

London dispersion forces are the weakest.

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12
Q

True or false: London dispersion forces occur between all molecules.

A

True.

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13
Q

Are London forces temporary ?

A

Yes, London forces are temporary as the occur randomly as there are various instances of unequal distribution of electrons around any given nuclei, creating temporary poles.

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14
Q

Are London forces more significant on smaller molecules?

A

No they are not.

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15
Q

What do dipole dipole forces do ?

A

They hold polar molecules together.

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16
Q

A partially positive side attracts the partially negative side of another molecule. Which force is this ?

A

The dipole dipole forces.

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17
Q

Hydrogen bonding only occurs between what molecules ?

A

When H is attracted to either N, O or F.

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18
Q

Water molecules are attracted to each other by was intermolecular force ?

A

Hydrogen bonding

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19
Q

A molecule that fears water is _______.

A

Hydrophobic .

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20
Q

What is the auto ionization of water ?

A

The production of a H3O+ molecule.

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21
Q

Do acids or bases have an increased level of H30 when dissolved in water.

A

Acids.

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22
Q

There is an increased concentration of OH- molecules in what solutions ?

A

Bases.

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23
Q

What is a buffer ?

A

A chemical balancing system that can donate an H+ ion when required and that can remove a them when there are too many in a solution.

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24
Q

What are the four classes of macromolecules?

A

Carbohydrates, fats, proteins and nucleic acids.

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25
Q

The removal of an H+ ion from one subnit and an OH- from another subnit is what process ?

A

Dehydration Synthesis

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26
Q

Dehydration synthesis is anabolic because …

A

It absorbs energy and constructs a larger molecule.

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27
Q

The breaking of a macromolecule into their subnits through digestion is what process ?

A

Hydrolysis.

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28
Q

In hydrolysis, what is used to break the covalent bond?

A

A water molecule.

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29
Q

Why is hydrolysis a catabolic reaction?

A

Due to the releasing of energy through the breaking down of macromolecules.

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30
Q

What are the three types of carbohydrates?

A

Monosaccrides, oligosacchrides, and polysaccharides.

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31
Q

Monosacchrides are _______ or _______ .

A

Aldehydes or ketones.

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32
Q

A single carbon chain depicts what type of carbohydrate?

A

A Monosaccharide.

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33
Q

Define Glycosidic linkages.

A

Covalent bonds that are responsible for holding monosaccharides to one another that are formed by condensation reactions.

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34
Q

What process must occur to create a oligosaccharide?

A

Dehydration synthesis.

35
Q

Maltose is composed of what and is held together by what linkage?

A

Glucose and glucose, 1-4 linkage

36
Q

What is sucrose composed of and what type of linkage holds it together?

A

Glucose and fructose, 1-2 linkage.

37
Q

What molecule is composed of glucose and galactose and is held together by a 1-2 linkage?

A

Sucrose

38
Q

A complex carbohydrate is what type of carbohydrate?

A

A Polysaccharide.

39
Q

What are the two main purposes of polysaccharides?

A

Structural support and energy support.

40
Q

Cellulose and chitin serve what purpose?

A

Structural support.

41
Q

Glycogen and starch serve what purpose?

A

Energy storage.

42
Q

What happens to excess glucose ?

A

Enzymes in the chloroplast bind excess glucose together to create starch.

43
Q

What is the main differences between amylose an amylopectin?

A

Amylose is in branches where as amylopectin branches at 1-6 linkages.

44
Q

Glycogen had a 1-4 glycosidic linkage, and branches of with 1-6 linkages, however, glycogen has several more branches than amylopectin allowing it to…

A

Hydrolyze at a much faster rate, thus allowing a greater release of energy.

45
Q

Humans store what in their muscles for quick release of energy ?

A

Glycogen

46
Q

Cellulose differs from starch in what ways ?

A

It has beta glycosidic linkages and is this used for support instead of energy.

47
Q

What are lipids composed of ?

A

Carbon, hydrogen and oxygen.

48
Q

Tryglycerols are composed of what ?

A

3 fatty acids attached to one glycerol.

49
Q

A fat with only single bonds having the max number of hydrogen atoms is what type ?

A

A saturated fat.

50
Q

An unsaturated fat has what characteristics?

A

There is atleast one double bond, meaning it does not carry its max number of hydrogen atoms.

51
Q

A polyunsaturated fat differs from an unsaturated fat I’m what way?

A

Containing multiple double bonds.

52
Q

Functional molecules are what type of macromolecule ?

A

A protein.

53
Q

What is a biological catalyst?

A

An enzyme.

54
Q

Define conformation:

A

Final 3D shape of a protein after sequencing the poly peptide.

55
Q

How many amino acids are considered necessary?

A

20 amino acids.

56
Q

How many amino acids are considered essential?

A

8 amino acids.

57
Q

The amide linkage that holds together amino acids in polypeptides are considered what?

A

Peptide bonds.

58
Q

The sequence of amino acids in a polypeptide strand is what structure ?

A

The primary structure.

59
Q

Hydrogen bonding causes could and folds the polypeptide strand is what structure?

A

The secondary structure.

60
Q

An Alpha helix is …

A

A tight coil formed by h bonds.

61
Q

How are beta pleated sheets formed?

A

They are formed between parallel stretches of a polypeptide.

62
Q

What is the tertiary structure of a protein?

A

The supercoiling of a poly peptide by side gain interactions.

63
Q

What is a disulfide bridge?

A

Covalent bond between cystein residues in a polypeptide that stabilizes tertiary structure.

64
Q

Quaternary structure involves …

A

Two or more poly peptide subnits coming together to form a fictional protein.

65
Q

When can a protein be denatured ?

A

In high temp and pH changes.

66
Q

What does DNA do ?

A

It instructs the creation of an organism.

67
Q

What bases does DNA contain ?

A

A, T, C &G

68
Q

What bases does RNA contain ?

A

A, U, C & G

69
Q

What does RNA do?

A

It reads and transports the protein building apparatus to the cell.

70
Q

ATP is responsible for what ?

A

It drives all energy requiring processes in the body.

71
Q

Chemical Reactants < end products

A

Endergonic reaction.

72
Q

Exergonic reaction means that …

A

The products have less chemical potential energy than the reactants.

73
Q

Define phosphorylation:

A

The process of attaching a phosphate group to an organic molecule, this rendering it more reactive.

74
Q

What is a redox reaction?

A

A chemical reaction involving the transfer of one or more electrons from one atom to another where oxidization and reduction occur.

75
Q

Oxidization occurs to the …

A

Reducing agent.

76
Q

The oxidizing agent…

A

Reduces the substance.

77
Q

What speeds up a reaction by lowering activation energy?

A

An enzyme.

78
Q

A substrate is what ?

A

The reactant that the enzyme acts upon.

79
Q

What is the site where the enzyme binds to?

A

The active site.

80
Q

The induced for model states that ..

A

The protein molecule will change it’s shape so that it better fits the enzyme.

81
Q

Competitive inhibitors:

A

Substance that competes with the enzyme for a substrates binding site.

82
Q

Non competitive inhibitors:

A

A substance that binds to a binding site that is located away from the active site, causing the change in shape of the enzyme and loss of affinity for its substrate.

83
Q

Define Allosteric Site:

A

A receptor site that is away from the active site that binds to substrates that allow for inhibition or stimulation of an enzyme.

84
Q

What is feedback inhibition?

A

A method of metabolic control I’m which a product that has been formed later in the process of a sequence of reactions allosterically inhibits an enzyme that catalyze a a reaction early in the sequence.

Biology (6 decks)

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