Molecules of living systems (6.1) Flashcards

1
Q

Organic compounds

A

macromolecules containing very strong carbon-hydrogen bonds that can bond to lots of other carbon

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

Carbon chains

A

Forms the backbone of organic compounds. These skeletons can vary in length, branching, double-band position and presence of rings

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

Functional groups (7)

A

chemical patterns added to hydrocarbons to make macromolecules
(Hydroxyl, Methyl, Carboxyl, Carnonyl, amino, phosphil, Sulfhydryl)

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

Hydroxyl

A

polar (-OH)
R - O - H

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

Carboxyl

A

Acidic (-COOH)
R - C = O
\
OH

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

Carbonyl

A

Polar (-CO)
R
\
C = O
/
R

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

Amino

A

Basic (-NH2)
H
/
R - N
\
H

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Phosphil

A

Acidic (-PO4)
O
||
R - O - P - OH
|
OH

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

Biomolecule

A

Chemical compound found in living organisms

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

Essential Elements

A

CHONPS

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Monomer

A

Small single units that can bond to others to corm chains

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

Polymer

A

Larger molecules made of bonded monomers

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

Dehydration Synthesis

A

Removes H2O to allow for bonds

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

Hydrolysis

A

Adding H2O to break bonds

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

Carbohydrates Function

A

Energy release and storage in the body for movement and growth.

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

Monosaccharides examples

A
  • Glucose, Fructose and Galactose - They release energy quickly and have the same amount of atoms but in different structures (they are Isomers of each other)
  • C12H13O14
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Disaccharides

A

“Two Sugars” formed when two monosaccarides link together using dehydration synthesis.
(Ex: Glucose + fructose = Sucrose
Glucose + Fructose = Maltose)

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

Polysaccharides(3)

A
  • “Many Sugars” long chains of monosaccharides linked by glycosidic bonds
  • made from dehydration synthesis reactions
  • Ex: Amylopectin, Amylose, Cellulose, Glycogen
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Amylopectin

A
  • Long branched chain
  • lets glucose release quickly
  • starch
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Amylose

A
  • Long branched chain
  • coiled to make it compact for storage
  • starch
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Cellulose

A
  • long straight chains
  • can form hydrogen bonds
  • Good support for cell walls
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Glycogen(3)

A
  • Highly branched with many side branches
  • Very quick release of glucose
  • In animals
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Lipids

A

Macromolecule insoluble in water, found in fats, oils waxes and hormones

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Fatty acids

A
  • Lipid monomers
  • Consist of carboxyl group joined to a hydrocarbon chain
  • can be saturated or unsaturated
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Saturated Fatty acid
No double carbon bonds (no C=C)
26
Unsaturated fatty acids
At least one double carbon bond (C=C)
27
Trans Unsaturated fatty acids
Straight structure, double bond
28
Cis Unsaturated fatty acids
Bent structure, double bond
29
Triglycerides Formation
Dehydration synthesis Glycerol + 3 fatty acids ---> triglycerides + 3 water molecules
30
Triglycerides traits (5)
- Long term stores for energy - Energy released when they are broken down - Stored as fat (good for isolation in the cold) - insoluble in water - Held by ester bond
31
Phospholipids traits (3)
- Make up the cell membrane - forms a bilayer with the hydrophilic tails facing inwards and hydrophilic heads facing outwards - Structure has a phosphate group bonded to glycerol (makes head) , bonded to two fatty acids (the tails)
32
Hydrophilic
Water loving
33
Hydrophobic
Water hating
34
Waxes traits and Examples (3)
- Long chains of hydrocarbons - Water repellent Ex: plant leaves to prevent water loss, animals have earwax to clean and protect ears
35
Steroids traits and examples (4)
- Basic structures of four rings of carbon atoms - Insoluble i water - basis of many hormones - Ex: Testosterone and Estrogen
36
Cholesterol traits and examples (3)
- Type of steroid - key component of cell membrane - two types: LDL and HDL
37
LDL Cholesterol (4)
- Low density lipoproteins - bad cholesterol - caused by saturated and trans fats - causes fatty deposits in arteries (restricts blood flow and causes heart disease and stroke)
38
HDL Cholesterol (2)
- High density lipoprotein - good Cholesterol
39
Proteins
Type of macromolecule made of amino acids
40
Amino acids (2)
- Protein monomers - Contain Carboxyl and amino groups - CHON
41
Dipeptides
two amino acids joined by a peptide bond formed through dehydration synthesis
42
Polypeptides
Chains of amino acids joined by peptide bonds formed through dehydration synthesis
43
Essential amino acids
- Cannot be made in the body - must be obtained from food - 9/20 of amino acids are essential amino acids
44
Primary structure of polypeptides (5)
- Polypeptide chain - sequence of amino acids joined by peptide bonds - Coded for by genes - Made through protein synthesis - varies in length
45
Secondary structure of polypeptides (4)
- Polypeptide chain gets folded - form alpha helices and beta pleated sheets - folding made possible by hydrogen bonds between carbonyl and amino groups of different amino acids
46
Alpha Helix
Polypeptide chain is coiled into a ribbon-like helix (curl)
47
Beta Pleated sheet
Polypeptide chain is folded into segments that line up be side each other ( n shape)
48
Tertiary structure structure of polypeptides (
- Polypeptide Alpha Helix and Beta pleated sheet gets folded into 3D structure (tangle) - Based on R group reactions - Hydrophobic will "hide" on the inside - Hydrophilic portions will be on the outside - Held by ionic and hydrogen bonds
49
Quaternary structure of polypeptides (5)
- two or more polypeptide chains bond together (bigger tangle) - Each chain is a subunit - Held by hydrogen and ionic bonds
50
Digestive enzymes
Break down food molecules in the stomach so they can be absorbed in the small intestine Ex: lipase, amylase, pepsin, lactase
51
Contractile Proteins
Filaments in the muscles that slide over each other to allow animals to move Ex: Actin and Myosin
52
Transport Proteins
Move substances around the body in the blood or lymph systems Ex: hemoglobin binds to oxygen
53
Defense proteins
White blood cells produce antibodies to fight of harmful pathogens. The antibodies can neutralize it or mark it for destruction
54
Hormones
Regulate functions of the body by traveling in the blood to target organs Ex: insulin controls blood glucose levels
55
Structural proteins
build different structures in the cells in our bodies like the cytoskeleton Ex: keratin, which makes hair
56
Storage proteins
Provide a source of food for developing embryos in some animals like chickens, and for seedlings in some plants Ex: albumin in eggs
57
Nucleic Acids
Type of macromolecule that carry important information. There are 2 types: DNA & RNA
58
Nucleotides
Nucleic acids monomers
59
DNA
Deoxribonucleic Acid, found in the nucleus of the cell
60
RNA
Ribonucleic Acid, found in the nucleus and cytoplasm
61
Nucleotide structure
CHONP 1 phosphate group Nitrogenous base (DNA has 4, RNA has 1) Pentose sugar
62
DNA Nitrogenous bases
Adeine, Thymine, Guamine, cyosine A --> T G --> C
63
RNA Nitrogenous bases
Adenine, Uracil, Guamine, cyosine
64
Pyrimidines
Nitrogenous bases with single rings (Thymine and Cyosine)
65
Purines
Nitrogenous bases with two rings (Adenine and Guamine)
66
DNA Structure (4)
- double heilix - has base pairs - Long molecule - Anti-parallel
67
DNA Functions
- Contains genetic information - Passes on to offspring - Controls cells activities
68
RNA Structure
- single stranded - shorter than DNA - broken down quickly
69
RNA functions
- various functions - important in protein synthesis
70
Transfer RNA
carries amino acids
71
Messanger RNA
used to build proteins
72
Ribsomal RNA
makes up part of ribosomes
73
Enzymes traits (4)
- Biological catalysts - speed up reactions in the body without being used up - they lower activation energy for reactions - have distinct shapes because of their tertiary structure
74
How do enzymes work (4)
1. float around 2. collide with a substrate that matches their activation site 3. Substrate binds to the active site 4. Substrate bonds broken and are released, enzyme remains unchanged (can be reversed where substrates are rebonded)
75
Can enzymes change shape?
Yes, active sites can change to better fit a substrate (AKA induced fit)
76
pH affect on enzymes (3)
- affects how well it functions - Different enzymes have optimal pH where it works best - When pH is too far outside of the range, the enzyme becomes denatured
77
Denatured
When an enzym's hydrogen bonds that give it its shape is disrupted and changes the active site shape. Can be permanent
78
pH scale
0-6 = acidic 7 = neutral 8-14 = Basic
79
Temperature affect on enzymes
- Different organisms have different environmental and body temperatures - more heat means more kinetic energy which means faster rate of reaction - too hot causes denatureing of the enzyme
80
competitive inhibitors
bonds to the active site of an enzyme in direct competition with substrates
80
non-competitive inhibitors
- a molecule that can bind to another site on the enzyme - causes active site to change shape - can no longer catalyze reactions
81
Enzyme concentration
As the concentration increases the rate of reaction increases and then plateaus as all the substrates are all catalyzed
82
Substrate concentration
As the concentration increases the rate of reaction increases and then plateaus as all the active sites are occupied
83
Cofactors
molecules that attach temporarily or permanently to help enzymes work at their optimum
84
Iodine test
Tests for complex carbohydrates Positive: Blue - black
85
Benedict's solution
Tests for simple carbohydrates Positive: Yellow-green, orange
86
Biuret Reagent
Tests for proteins Positive: violet - purple
87
Translucence test
Tests for lipids Positive: see through marks on a paper bag
88
Sudan III
Tests for lipids Positive: clumping
89
Sudan IV
Tests for lipids Positive: pink ---> red