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Biology > The Chemistry Of Living Things > Flashcards

The Chemistry Of Living Things Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What does the octet rule state?

A

Atoms prefer to have 8 valence electros

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2
Q

What is the reactivity of atoms when stable?

A

Low

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3
Q

What manes an atom stable

A

Fulfilling the octet rule, having 8 valence electrons

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4
Q

What is the reactivity of an unstable atom & why?

A

It is high because it wants to react to fulfill the octet rule

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5
Q

A covalent interractions/ bonds strong or weak?

A

Strong

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6
Q

What are weak interactions?

A

Non-covalent

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7
Q

What happens when non-covalent interactions occur in large numbers?

A

They create a cumulative effect

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8
Q

What are the 4 types of weak interactions that typically occur in organisms ?

A

Ionic interactions, hydrogen bonds, van de waals interactions & hydrophobic interactions

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9
Q

Definition of ionic interactions

A

Electrostatic interactions between charged particles

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10
Q

Where are ionic interactions strongest?

A

In a vacuum medium

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11
Q

Where are ionic interactions weaker? & why

A

In aqueous environments, water tends to separate the two charges making them further apart because water also interacts w/ the charges which makes then less attracted to each other

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12
Q

Where do ionic interactions typically occur is ex humans?

A

In amino acids

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13
Q

When do hydrogen bonds occur

A

When hydrogen is covalently bound to other atoms

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14
Q

Where do hydrogen bonds typically occur in biological systems?

A

In DNA base pairing

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15
Q

Definition of Van her waals interactions

A

Attraction between 2 uncharged atoms due to permanent/ transient/ induced dipoles

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16
Q

3 most common Van her walls interaction

A

Dipole-dipole, dipole-induced dipole & induced-dipole- induced-dipole

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17
Q

Definition of hydrophobic interaction

A

Intractor between non-polar molecules in an aqueous environment, exclusion g wall

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18
Q

4 Major bio molecule in organisms

A

Proteins, nuclei acids, carbohydrates/ polysaccharides & lipids

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19
Q

What are proteins?

A

Polymers built of monomer units called amino acids, chain of amino acids

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20
Q

What are some functions of proteins in the body & other organisms?

A

Muscle contraction, hormones, enzyme activity, storage, growth, repair etc.

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21
Q

When are proteins functional?

A

Only when they are put together in their proper structure & form

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22
Q

How many amino acid are there in the human body & how many are essential & non-essential? What does it mean you them to be essential or not?

A

20, 9 essential & 11 non- essential, essential have to be consumed & non- essential can be made by the body

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23
Q

What is it called when a Carbon has 4 differs bonds to it?

A

Chiral center

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24
Q

What do all amino acids have in common when looking at the chem of it

A

They all have a central Carbon, amino group, carboxyl group, they only differ in their R group

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25
Q

What is 2 units of amino acids connected called?

A

Dipeptide

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26
Q

What is 3 units of amino acids connected called?

A

Tripeptide

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27
Q

What is a chain of amino acids connected called when there are more than 10 units?

A

Polypeptide

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28
Q

What kind of bonds do amino acids make? & what is typical connected to what?

A

Peptide bonds, typically carboxyl group connected to amino group

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29
Q

What are the ends of an amino acid called?

A

End w / carboxyl group is C terminus end w/ amino group is N terminus

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30
Q

What end are chains of amino acids read from & to?

A

From N terminus to C terminus

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31
Q

What are the 4 kinds of protein structures?

A

Primary ( amino acid sequence) secondary structure ( alpa- helix / beta - plated sheets) tertiary structure (3d) & quatenary structure ( multiple polypeptides )

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32
Q

What protein structure is the only fully functional?

A

Quaternary structure

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33
Q

What are the two types of nuclei acid?

A

DNA & RNA

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34
Q

What kind of monomers are nucleic acids composed of?

A

Nucleotides

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35
Q

What is the back bone of DNA called?

A

Phosphate sugar backbone

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36
Q

What are the two types of pentuse sugar in nuclei acids

A

Ribose (RNA) & deoxirisose (DNA)

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37
Q

What are the 3 chemical components of nucleic acids?

A

Nitrogenous, pentose sugar, phosphate

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38
Q

What chemical group are the basepairs in DNA double helix?

A

Nitrogerous

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39
Q

What are the different types of nitrogenous base pairs & what defines them

A

Purine ( 2 nitrogenous rings, adenine & guanine), pyridines (only has 1 ring, thymine (DNA), cytosine & uracil(RNA))

40
Q

What 3 elements do carbohydrates consist of?

A

Oxygen, hydrogen & Carbon

41
Q

What is the simplest form of carbohydrates?

A

Monosaccharides

42
Q

What are the 2 main functions of carbonhydates?

A

Energy & storage of energy

43
Q

What can monosaccharides form & how?

A

Disaccharides & polysaccharides Via glycosidic bonds

44
Q

What are some common disaccharides?

A

Sucrose ( glucose+ fructos), lactose ( glucose + galactose) & maltose (glucose+glucose)

45
Q

What are some common polysaccharides & their main function?

A

Celulose, starch & glycogen (storage of energy)

46
Q

What are lipids

A

A diverse group of bio molecous that are insoluble in water

47
Q

What are enzymes?

A

Biological catalyst which speeds up the chemical reaction but is not consumed by the reaction. Most are proteins

48
Q

How do reactions in the body start?

A

Spontaneously, they don’t need a catalyst to happen but just to speed the reaction up

49
Q

Primary ways to increase reactions in body

A

Temperature & enzymatic catalyst

50
Q

How much does enzymes speed up reactions?

A

10^5 - 10^7

51
Q

Do enzymes increase the number of products?

A

No, only the speed

52
Q

What does enzymes cover?

A

Activation energy / Ea

53
Q

Do enzymes change the position of the equilibrium?

A

No, only the rate

54
Q

What are enzyme inhibitors?

A

Compounds that bind to the enzymes & lower enzymatic activity

55
Q

Examples of enzyme inhibitors

A

Drugs & toxins

56
Q

Common types of reversible inhibition (name 4)

A

Competitive inhibition, pure non-competative inhibition, mixed non-competitive inhibition & allosteric/ uncompetitive inhibition

57
Q

How do competitive inhibitors work?

A

They resemble normal substrates (what is meant to react w/the enzyme) & binds to the active site on the enzyme. Binding of inhibitor or substrate is exclusive. Concentration increases the chances of the inhibitors binding instead of the substrate

58
Q

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

A

Competitive binds to active site where non -competative binds away from it.

59
Q

Can both non- competitive inhibitor & substrate bind to enzyme at the same time?

A

Yes

60
Q

Difference between pure & mixed non-competitive inhibitors

A

Pure binds far from activation site & changes enzyme conformation
Mixed binds close to activation site & affects the affinity of the enzyme for the substrate

61
Q

When does uncompetitive inhibition occur?

A

When inhibitors bind to the enzyme-substrate complex (Es)

62
Q

What are allosteric enzymes?

A

Effector molecules, can effect positively (activators) or negatively (inhibitors)

63
Q

What are the 2 sites on enzymes?

A

Active site & regulatory site

64
Q

What factors can effect enzymes?

A

Temp & pH

65
Q

What are cofactors?

A

Non-protein part of enzyme needed for reaction to take place

66
Q

Name common cofactors

A

Nad ( nicotinamide adenine dinuleotide), folic acid & vitamin c

67
Q

What is anabolic process?

A

Building of larger molecules from smaller ones

68
Q

What is lost when making monomers into polymers?

A

Water, so if 5 monomers are connected 4 h2o molecules are lost

69
Q

Is water polar or non-polar?

A

Polar

70
Q

What kind of bonds does water molecules form with other water molecules?

A

Hydrogen bonds

71
Q

Why is water essential for life?

A

Good solvent: can dissolver molecules
Ice is less dense than water which allows for aquatic life
High heat capacity making it hard to heat up allowing for life to withstand changes in temp
Biological reactions take place in water
Cohesion of water molecules allows water to stick together which is important for water to move upwards in plants

72
Q

Why does water have a high heat capacity?

A

Hydrogen bonds requiring more energy to brake

73
Q

What is the latent heat of vaporization? & why is it relevant to biology

A

The amount of heat that must be transferred to a liquid substance at it’s boiling point to turn into gas
It allows for cooling when sweating

74
Q

Does water have high or low heat of vaporization?

A

High

75
Q

Does water have high or low specific heat capacity?

A

High

76
Q

In what form is water most dense?

A

Liquid

77
Q

What is a condensation/dehydration reaction?

A

Synthesis reaction

78
Q

What happens during a condensation/dehydration reaction?

A

2 reagents combine covalently
Water is released: one water molecule is released for every bond formed
Requires enzymes to catalyse

79
Q

What is a hydrolysis reaction?

A

Decomposition reaction

80
Q

What happens during a hydrolysis reaction?

A

A bond is broken to yield 2 products
Water is used to brake the bond: one water molecule can break 1 bond
Require enzymes

81
Q

How does a phosphorylation reaction go?

A

Add a phosphate Pi to a molecule (conecently) to give extra 2 negative charges

82
Q

What enzymes perform phosphorylation?

A

Kinases

83
Q

Where is the only place kinases work?

A

Inside the cell as ATP is required for phosphorylation to take place

84
Q

What is the reverse of phosphorylation called?

A

Dephosphorylation

85
Q

What happens in dephosphorylation?

A

A phosphate group is removed, removes the -2 charges

86
Q

What enzyme is used for dephosphorylation?

A

Phosphates ( & water)

87
Q

Is the phosphate removed during dephosphorylation added back to ATP?

A

No

88
Q

Is Nadh → nad+ an oxidation or reduction?

A

Oxidation

89
Q

Is nad+ → nadh an oxidation or reduction?

A

Reduction

90
Q

What processes add carbon dioxide to the atmosphere

A

Combustion, aerobic respiration (both plants and animals) and the activity of decomposers

91
Q

What processes remove carbon dioxide from the atmosphere

A

Photosynthesis

92
Q

What processes add oxygen to the atmosphere

A

Photosynthesis

93
Q

What processes remove oxygen from the atmosphere

A

The activity of decomposers, combustion, and aerobic respiration (in both plants and animals)

94
Q

What is catabolism ?

A

Breaking apart a molecule, typically to release energy

95
Q

What is anabolism?

A

Taking 2 smaller molecules & making a bigger molecule out of them. Uses energy

96
Q

What is gluconeogehesis? & where does occur

A

Process where body produces glucose from non-carbohydrate sources such as amino acids, lactate & glycerol
Primarily in liver & to lesser extent in the kidneys

97
Q

Name for breakdown of glycogen

A

Glycogenolysis

Biology (7 decks)

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