Unit 1- Flashcards
(116 cards)
1
Q
-OH
A
Hydroxyl
Polar so soluble in h2o
2
Q
Where are hydroxyls found?
A
Sugars and alcohols
3
Q
-COOH
A
Carboxyl
Polar so soluble in H2O
4
Q
What does a carboxyl do to a molecule?
A
Makes it acidic
5
Q
-CO
A
Carbonyl
6
Q
Where is a carbonyl found?
A
On aldehydes and ketones
7
Q
-NH2
A
Amino
Found on amino acids
8
Q
What’s does an amino do to a molecule?
A
Makes the solution basic
9
Q
PO4 2-
A
Phosphate
10
Q
Where are phosphates found?
A
Found on nucleotides and nucleic acids.
11
Q
What do phosphates help with?
A
Energy transfer
12
Q
-SH
A
Sulfhydryl
13
Q
Where are sulfylhydryls found?
A
Found in cellular molecules
14
Q
Triose
A
Sugar with 3 carbon atoms. C3H6O3
15
Q
Pentose
A
Sugar with 5 carbon atoms. C5H10O5
16
Q
Hexoses
A
Sugar with 6 carbon atoms C6H12O6
17
Q
Aldoses
A
Carbonyl located on the last carbon in the chain
18
Q
Ketoses
A
Carbonyl located on a carbon in the middle of the chain
19
Q
4 types of macromolecules
A
Carb protien lipid nucleic acid
20
Q
Monomer of carbs
A
Monosaccharides
21
Q
Monomer of lipids
A
Glycerol and fatty acids
22
Q
Monomer of protien
A
Amino acids
23
Q
Monomer of nucleic acid
A
Nucleotides
24
Q
What happens when pentoses and hexoses enter water
A
They turn from linear to cyclic
25
Starch
(Poly) formed in chloroplasts
26
Form of starch
20% straight amylose
| 80% branches amylopectin
27
Glycogen
(Poly) more branched than amylopectin. Energy storage molecule found in liver and muscle cells. Hydrolysis to glucose during physical exercise
28
Cellulose
Straight chain found in cell wall. Humans can't digest it
29
Chitin
Found in cell wall of fungi and exoskeleton of insects and crustaceans
30
Function of lipids
Store energy. Build membrane and other cell parts. Chemical signals (hormones)
31
Families of lipids
Fat wax steroid phospholipid
32
Energy in 1 g of fat and carbs
```
Fat = 38kj
Carbs = 17 kj
```
33
Fats are stored in animals by
Droplets in cell of fat tissue. Thermal insulation in penguins.
34
Fats are stored in plants by
Stored in seeds as oil
35
Saturated fat
Single bonds between carbon atoms
36
Unsaturated fat
One or more double bonds between c atoms
37
Animal fat
Saturated molecules fit tight together so solid at room temp.
38
Plant oil
Polyunsaturated so bends in molecules make them not fit together. So liquid at room temp
39
Difference between glucose and galactose
The oh on carbon 4 is down on glucose. The oh on carbon 4 is up on galactose.
40
Steroid example
Cholesterol. Testosterone. Estrogen.
41
Primary protein structure
Unique sequence of amino acids in the polypeptide chain. Under the control of DNA
42
What is a residue
Each amino acid in the polypeptide chain
43
Secondary protein structure 2 types
Alpha helix and beta pleated sheets
44
Alpha helix
Hydrogen bonds form between the O of a carboxyl group and the H of a different amino. Repeated H bonds shape the polypeptide into a coil.
45
Alpha helix example
Alpha keratin
| Found in hair
46
Beta pleated sheets
When 2 polypeptide chains lie parallel to each other and Hydrogen bonds form between the carboxyl and adjacent amino strand
47
Beta pleated sheet example
In spider silk and can stretch 40 % before breaking while steal will only bend 8%
48
Tertiary structure
The protein folds because various points on the structure are attracted to eachother. Strongest bonds are disulfide bridges. There are also weak ionic bonds and hydrophobic bonds.
49
Quaternary structure
When 2 or more amino acid chains link together to make a more complex protien.
50
Conjugated protien
Protien containing non protien material.
51
Prostetic group
The non protien part in a conjugated protein
52
Waxes
Long fatty acids liked to alcohols or carbon rings. Pliable and hydrophobic so then waterproof
53
Example of waxes 3
Cutin- epidermal cell of plants to conserve h2o
Birds- wax keeps feathers dry
Bees-beeswax used for honeycomb
54
Functions of proteins 4
Enzymes-catalysts
Immunoglobulins-protect against pathogens
Transport-hemoglobin or phloem
Structure-keratin collagen fibrin
55
When dissolved in water what happens to some proteins
They become amphipratic which is acidic and basic zwitter ions
56
3 types of amino acids
Polar non polar and charged
57
Polar amino acid
Hydrophilic. Side chains contain oxygen which makes them very electronegative
58
Non polar amino acid
Hydrophobic side chains are mostly carbon and hydrogen
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Charge amino acid
Acidic or basic. Side chains have carboxyl or amino groups
60
What is the 3D shape of a protien known as and what is it determined by
Confirmation
| Sequence of amino acids
61
Polypeptide
Multiple amino acids linked together
62
What are amino acids held together by
Peptide bonds
63
Structural protien
Framework ex hair
64
Defensive protien
Infection fighters. Ex. Antibodies
65
Signal proteins
Messenger. Ex hormones
66
Carrier proteins
Transport all materials. Ex hemoglobin
67
Recognition/ receptor
Cell markers. Ex. Major histocomparibility complex
68
Enzyme protien
Catalyst ex amylase
69
Motile protien
Movement ex actin and myosin
70
Transcription to amino acids order
DNA transcribed to mRNA. mRNA translated to protien at ribosomes. During translation amino acids are linked by peptide bonds
71
A terminus
Free amino group at end of polypeptide
72
C terminus
Free carboxyl at end of polypeptide
73
How many essential amino acids are there
9 that must be ingested for survival. But there are 20 total but the rest are made by the body
74
Plasmodesmata
In plants. Tiny cell receptors that act like bridges of cytoplasm that pass through adjacent cell walls and link them allowing rapid exchange of materials
75
Belt desmosomes
Line body cavities Ike the mouth and form protective layers like the skin
76
Spot desmosomes
Hold cells together and anchor the intermediate filaments of the cytoskeleton. Found in cells of tissues that have a lot of wear and tear like outer layers of skin
77
Hemidesmosome
Attaches a cell to extra cellular matrix
78
How does communication occur thru cells?
Gap junctions. They are protien lined pores that connect adjacent cells
79
Integral membrane proteins
Anchored in place. Projecting regions must have polar R groups. Allows different things to move through
80
Integral protien that allows water to travel through it
Aquaporin
81
Hydroxyl + hydroxyl
Ether
82
Hydroxyl + carboxyl
Ester
83
Carboxyl + carboxyl
Anhydride
84
2 phosphoric acids
Phosphate annhydride
85
Hydroxyl + phosphoric acid
Phosphate ester
86
How to develop a protien
Add them together int he order they're given and the number of bonds is he number of waters produced
87
Protein denaturation
Results in change of 3 D shape of a protein. Loses its function
88
Causes of denaturation
Temperature ph ionic concentration and heavy metal salts
89
If the denaturing agent is removed it may
Return to normal or remain denatured because the damage was too much
90
Dangerous denaturation examples
Fever causes denaturation of brain causing seizure and coma
91
Helpful denaturation examples
Hair styling chemicals and heat used to curl or straighten hair
92
Competitive inhibition
Enters active site and blocks substrate from binding. Can be reversed by increased substrate concentration
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Non competitive inhibition
Attaches to enzyme but not at active site. Causes change of shape and loses affinity. Or affects part of enzyme that's active in catalysis. Non reversible.
94
Gibbs free energy equals
G reactants -G products
95
Lose electrons
Oxidation
96
Gain electrons
Reduction
97
Negative G
Exergonic so catabolic
98
Positive G
Endergonic so anabolic
99
Glycoproteins
I'm phospholipid bilayer. Proteins attach carb chains. Help with cellular recognition and immune response. Receptors for hormones
100
Glycoproteins and glycolipids
Together they stabilize the phospholipid bylayer
101
Cholesterol in fluid mosaic model
Lipid. Regulates membrane fluidity
102
Glycolipids
Surface receptors
103
Integral protien in bilayer
Control entry and removal of molecule from the cell
104
Induced fit model
Functional group on substrate comes close to functional group on amino acids at active site. Close interaction causes protien to change shape to better accommodate the substrate
105
Active site
Binds to substrate
106
Allosteric site
Binds a substance that may stimulate or inhibit the enzymes activity
107
Activator inhibitor
Binds to allosteric site and stabilizes active form of enzyme. Available to bind with substrate
108
Allosteric inhibitor
Binds to allosteric site. Stabilizes inactive form of enzyme. Active site will be unable to bind with substrate when enzyme is in inactive form
109
Feedback inhibition
Method of metabolic control. Product formed later in a sequence of reactions allosterically inhibits an enzyme that catalyzes a reaction earlier in the process. Happens when there's too much. So the body gives negative feedback and regulates itself.
110
Types of integral proteins 6
Hormone receptor, enzymes, electron carriers, passive transport, active transport pumps and attachment to cytoskeleton
111
Globular protein
Hemoglobin
112
Hyponatrimia
When there is excess body fluid in the body so it enters the cells and they expand too much. Dilutes Na+ serum.
113
When you have hyponatrimia
Less than 135 concentration of sodium ions in serum
114
Types of bonds in tertiary structures strong to weak
Disulfide bridge, h bonds, ionic bonds, hydrophobic bonds
115
Anabolic
Making of molecules
116
Catabolic
Breaking down of molecules
