Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

Biology > The Chemistry Of Living Things > Flashcards

The Chemistry Of Living Things Flashcards

(97 cards)

Start Studying
1
Q

What does the octet rule state?

A

Atoms prefer to have 8 valence electros

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What is the reactivity of atoms when stable?

A

Low

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What manes an atom stable

A

Fulfilling the octet rule, having 8 valence electrons

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

A covalent interractions/ bonds strong or weak?

A

Strong

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What are weak interactions?

A

Non-covalent

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

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

A

They create a cumulative effect

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Definition of ionic interactions

A

Electrostatic interactions between charged particles

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Where are ionic interactions strongest?

A

In a vacuum medium

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Where do ionic interactions typically occur is ex humans?

A

In amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

When do hydrogen bonds occur

A

When hydrogen is covalently bound to other atoms

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Where do hydrogen bonds typically occur in biological systems?

A

In DNA base pairing

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Definition of Van her waals interactions

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

3 most common Van her walls interaction

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Definition of hydrophobic interaction

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

4 Major bio molecule in organisms

A

Proteins, nuclei acids, carbohydrates/ polysaccharides & lipids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What are proteins?

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

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

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

When are proteins functional?

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

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

A

Chiral center

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
What is 2 units of amino acids connected called?
Dipeptide
26
What is 3 units of amino acids connected called?
Tripeptide
27
What is a chain of amino acids connected called when there are more than 10 units?
Polypeptide
28
What kind of bonds do amino acids make? & what is typical connected to what?
Peptide bonds, typically carboxyl group connected to amino group
29
What are the ends of an amino acid called?
End w / carboxyl group is C terminus end w/ amino group is N terminus
30
What end are chains of amino acids read from & to?
From N terminus to C terminus
31
What are the 4 kinds of protein structures?
Primary ( amino acid sequence) secondary structure ( alpa- helix / beta - plated sheets) tertiary structure (3d) & quatenary structure ( multiple polypeptides )
32
What protein structure is the only fully functional?
Quaternary structure
33
What are the two types of nuclei acid?
DNA & RNA
34
What kind of monomers are nucleic acids composed of?
Nucleotides
35
What is the back bone of DNA called?
Phosphate sugar backbone
36
What are the two types of pentuse sugar in nuclei acids
Ribose (RNA) & deoxirisose (DNA)
37
What are the 3 chemical components of nucleic acids?
Nitrogenous, pentose sugar, phosphate
38
What chemical group are the basepairs in DNA double helix?
Nitrogerous
39
What are the different types of nitrogenous base pairs & what defines them
Purine ( 2 nitrogenous rings, adenine & guanine), pyridines (only has 1 ring, thymine (DNA), cytosine & uracil(RNA))
40
What 3 elements do carbohydrates consist of?
Oxygen, hydrogen & Carbon
41
What is the simplest form of carbohydrates?
Monosaccharides
42
What are the 2 main functions of carbonhydates?
Energy & storage of energy
43
What can monosaccharides form & how?
Disaccharides & polysaccharides Via glycosidic bonds
44
What are some common disaccharides?
Sucrose ( glucose+ fructos), lactose ( glucose + galactose) & maltose (glucose+glucose)
45
What are some common polysaccharides & their main function?
Celulose, starch & glycogen (storage of energy)
46
What are lipids
A diverse group of bio molecous that are insoluble in water
47
What are enzymes?
Biological catalyst which speeds up the chemical reaction but is not consumed by the reaction. Most are proteins
48
How do reactions in the body start?
Spontaneously, they don't need a catalyst to happen but just to speed the reaction up
49
Primary ways to increase reactions in body
Temperature & enzymatic catalyst
50
How much does enzymes speed up reactions?
10^5 - 10^7
51
Do enzymes increase the number of products?
No, only the speed
52
What does enzymes cover?
Activation energy / Ea
53
Do enzymes change the position of the equilibrium?
No, only the rate
54
What are enzyme inhibitors?
Compounds that bind to the enzymes & lower enzymatic activity
55
Examples of enzyme inhibitors
Drugs & toxins
56
Common types of reversible inhibition (name 4)
Competitive inhibition, pure non-competative inhibition, mixed non-competitive inhibition & allosteric/ uncompetitive inhibition
57
How do competitive inhibitors work?
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
What is the difference between competitive & non- competitive inhibitors?
Competitive binds to active site where non -competative binds away from it.
59
Can both non- competitive inhibitor & substrate bind to enzyme at the same time?
Yes
60
Difference between pure & mixed non-competitive inhibitors
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
When does uncompetitive inhibition occur?
When inhibitors bind to the enzyme-substrate complex (Es)
62
What are allosteric enzymes?
Effector molecules, can effect positively (activators) or negatively (inhibitors)
63
What are the 2 sites on enzymes?
Active site & regulatory site
64
What factors can effect enzymes?
Temp & pH
65
What are cofactors?
Non-protein part of enzyme needed for reaction to take place
66
Name common cofactors
Nad ( nicotinamide adenine dinuleotide), folic acid & vitamin c
67
What is anabolic process?
Building of larger molecules from smaller ones
68
What is lost when making monomers into polymers?
Water, so if 5 monomers are connected 4 h2o molecules are lost
69
Is water polar or non-polar?
Polar
70
What kind of bonds does water molecules form with other water molecules?
Hydrogen bonds
71
Why is water essential for life?
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
Why does water have a high heat capacity?
Hydrogen bonds requiring more energy to brake
73
What is the latent heat of vaporization? & why is it relevant to biology
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
Does water have high or low heat of vaporization?
High
75
Does water have high or low specific heat capacity?
High
76
In what form is water most dense?
Liquid
77
What is a condensation/dehydration reaction?
Synthesis reaction
78
What happens during a condensation/dehydration reaction?
2 reagents combine covalently Water is released: one water molecule is released for every bond formed Requires enzymes to catalyse
79
What is a hydrolysis reaction?
Decomposition reaction
80
What happens during a hydrolysis reaction?
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
How does a phosphorylation reaction go?
Add a phosphate Pi to a molecule (conecently) to give extra 2 negative charges
82
What enzymes perform phosphorylation?
Kinases
83
Where is the only place kinases work?
Inside the cell as ATP is required for phosphorylation to take place
84
What is the reverse of phosphorylation called?
Dephosphorylation
85
What happens in dephosphorylation?
A phosphate group is removed, removes the -2 charges
86
What enzyme is used for dephosphorylation?
Phosphates ( & water)
87
Is the phosphate removed during dephosphorylation added back to ATP?
No
88
Is Nadh → nad+ an oxidation or reduction?
Oxidation
89
Is nad+ → nadh an oxidation or reduction?
Reduction
90
What processes add carbon dioxide to the atmosphere
Combustion, aerobic respiration (both plants and animals) and the activity of decomposers
91
What processes remove carbon dioxide from the atmosphere
Photosynthesis
92
What processes add oxygen to the atmosphere
Photosynthesis
93
What processes remove oxygen from the atmosphere
The activity of decomposers, combustion, and aerobic respiration (in both plants and animals)
94
What is catabolism ?
Breaking apart a molecule, typically to release energy
95
What is anabolism?
Taking 2 smaller molecules & making a bigger molecule out of them. Uses energy
96
What is gluconeogehesis? & where does occur
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
Name for breakdown of glycogen
Glycogenolysis

Biology (7 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions