bio- biochem Flashcards
(108 cards)
0
Q
Proton
A
Positively charged subatomic particle in an atoms nucleus
1
Q
8 Characteristics of life
A
Made of cells Use energy Ability to reproduce Respond to stimulus Maintain homeostasis Grow and develop Have DNA Change and evolve over time
2
Q
Neutron
A
Neutral subatomic particle in an atoms nucleus
3
Q
Electron
A
Negatively charged subatomic particle in electron shells
4
Q
Covalent bonds
A
When two atoms share their valence electrons and overlap their electron orbitals in order to complete the outermost orbital shell
5
Q
Valence electrons
A
Electrons in the outer shells that are used to covalently bond
6
Q
What makes a molecule organic?
A
The elements in it are covalently bonded Usually big Associated with living systems ALWAYS contain carbon SHNOPSi is commonly found in it
7
Q
SHNOPSi
A
Sulfur Hydrogen Nitrogen Oxygen Phosphorus Silicon
8
Q
Inorganic
A
Carbon dioxide and other molecules without carbon
9
Q
Carbon
A
Has 6 total electrons (4 valence)
Can form chains or rings (when it bonds)
Versatile
10
Q
How many elements can carbon potentially covalently bond with?
A
4 because it has 4 electrons in its outermost shell but can hold up to 8 in that shell– can bond with 4 other atoms to get 8
Can form single, double, or triple bonds, or rings
11
Q
What are Functional groups?
A
Cluster of atoms that determines the chemical reactivity and other characteristics of a molecule
12
Q
Name the functional groups
A
Hydrogen Hydroxyl Carboxylic acid Amino Phosphate Methyl
13
Q
Hydrogen group
A
-H
Polar or nonpolar (depending on which atom it is bonded to)
Involved in dehydration and hydrolysis reactions
Found in: almost all organic molecules
14
Q
Hydroxyl group
A
-O-H
Polar
Involved in dehydration and hydrolysis reactions
Found in: carbs, nucleic acids, alcohols,some acids, steroids
15
Q
Carboxylic acid group
A
=O
-C
-O-H
Acidic
Involved in peptide bonds
Found in: amino acids, fatty acids
16
Q
Amino group
A
-H
-N
-H
Basic
May bond an additional H+ to become positively charged
Involved in peptide bonds
Found in: amino acids, nucleic acids
17
Q
Phosphate group
A
H
O
-O-P=O
O
H
Acidic
Links nucleotides in nucleic acids
Energy-carrier group in ATP
Found in: nucleic acids, phospholipids
18
Q
Methyl group
A
H -C-H H Nonpolar Tends to make molecules hydrophobic Found in: many organic molecules, especially common in lipids
19
Q
Polar
A
Has opposite poles (ex: water)
Give away- one side has oxygen
20
Q
Electronegativity
A
Attracts electrons to its outer shell bc its v close to becoming stable (full electron outer shell)
But shares it evenly, doesn’t steal them
Ex: oxygen has 6 valence electrons, only 2 away
21
Q
Macromolecules
A
Huge molecules made up of smaller molecules
Macro=giant
Formed thru polymerization reactions
22
Q
Monomers
A
Subunit
Make up polymers
23
Q
Polymer
A
Multiple (3+) monomers together
24
Dimer
2 monomers
25
Polymerization reactions
Dehydration synthesis and hydrolysis
26
Dehydration synthesis/ condensation
Anabolic reaction
Monomers join together by removing a water molecule (H2O)
Partial negative end attracted to atrial positive end
27
Hydrolysis
Polymers broken down by breaking a water molecule into -H and -H-O and adding it to break the bond between monomers
28
4 categories of biological molecules
Carbohydrates
Lipids
Proteins
Nucleic acids
29
Carbohydrate composition
C, H and O in ratio of 1:2:1
| Ex: glucose is C6H12O6
30
Monosaccharides
Simple or single sugars
31
Disaccharides
Two linked monosaccharides
32
Polysaccharides
Long chains of monosaccharides
33
Isomer
Molecules with the same molecular formula but a diff structure
34
What's the only group of biomolecules that's isometric?
Carbohydrates
| Ex: C6H12O6 = fructose and glucose, but they have diff structures
35
Structure of monosaccharides
Back bone of 3-7 carbon atoms
Many -OH And -H functional groups
Ring shaped
36
Fate of monosaccharides inside a cell
Broken down for energy
OR
linked together by dehydration synthesis
37
Why are most small carbs water soluble
They have polar -OH functional groups
38
Sucrose (table sugar)=
Glucose+fructose
39
Lactose (milk sugar)=
Glucose+galactose
40
Maltose (malt sugar)=
Glucose+ glucose
41
2 types of polysaccharides
Storage polysaccharides
| Structural polysaccharides
42
Starch
Storage polysaccharide in plants
Polymer of glucose
Formed in roots and seeds as a form of glucose storage
43
Glycogen
Storage polysaccharide in animals
Polymer of glucose
Found in liver and muscles
44
Cellulose
Structural polysaccharide in plants
Polymer of glucose -- each alternate glucose is inverted
Found in cell walls of plants and some fungi
45
Why are cell walls indigestible for most animals?
Made of cellulose
The orientation of the bonds between glucose in cellulose (one is right side up, next is upside down, ...) --inverted pattern
46
Chitin
Structural polysaccharide in plants and animals
Polymer of modified glucose units
Found in outer coverings of insects, crabs, and spiders
Found in cell wall of some fungi
47
Lipids
Large chains of nonpolar hydrocarbons
| Hydrophobic and water insoluble
48
Major 4 functions of lipids
Long term energy storage
Waterproofing
Membranes in cells (ex: phospholipids)
Hormones (ex: estrogen and testosterone)
49
Fats and oils - structure
3 fatty acid subunits + glycerol join by dehydration synthesis to make a triglyceride
50
Fats and oils-purpose
Long term energy storage
51
What stores more energy- lipids or carbs? And why
Lipids -- more energy rich/ energy condensed than carbs
52
Saturated fats
Solid at room temperature
Fit as many hydrogens as possible
Mostly SINGLE bonds
fatty acid tails are straight
53
Problem with Saturated fats
Can become a plaque and stop your blood flow
54
Unsaturated fats
Liquid at room temperature
Less hydrogen atoms
DOUBLE bonds-- makes kinks in the tails
55
Problem with unsaturated fats
Unsaturated trans fats have been linked to heart disease
56
Waxes
Long hydrocarbon chains
Strongly hydrophobic
Highly saturated
57
Waxes-purpose
Form waterproof coatings and build honeycomb structures
58
Examples of where waxes are used
Waterproofing:
Leaves and stems of plants
Fur in mammals(especially marine)
Insect exoskeletons
59
Phospholipids
Form plasma membranes around all cells
60
Phospholipid structure
2 fatty acids + glycerol + short polar functional group
61
What is special about phospholipids (in terms of water solubility)?
It has polar heads (functional group) which are hydrophilic
| And nonpolar fatty acid tails which are hydrophobic
62
Steroid structure
Four carbon rings fused together
63
Steroids examples
Cholesterol (found in membranes of animal cells)
| Male and female sex hormones
64
Most important biomolecules
Proteins
65
Protein function
```
Structure
Movement
Defense
Storage
signaling
Catalyze reactions (most important)
```
66
Examples of structural proteins
Collagen in skin
| Keratin in hair, nails, and horns
67
Examples of movement proteins
Actin and myosin in muscles
68
Examples of defense proteins
Antibodies in bloodstream
69
Examples of storage proteins
Albumin in egg white
70
Example of signaling protein
Growth hormone in bloodstream
71
Example of catalyzing proteins
Enzymes
72
Protein composition
Chains of amino acids joined by dehydration synthesis
73
Amino acid structure
R group
Amino group-O-carboxylic acid group
H
74
R Group in amino acids
Variable group, differs in every amino acid
| Some are hydrophobic some are hydrophilic
75
If the R group is a cysteine..
Can form disulfide bridges
76
How are amino acids joined together to create a protein?
Dehydration synthesis creates a peptide bond between the carbon (from carboxylic acid group) and the nitrogen (amino group) of adjacent amino acids
O-H from carboxylic acid group and H from amino group are taken out as water
77
Importance of amino acids
The sequence, type, position, and number of amino acids determines the proteins structure and function
78
What happens if the positioning of R groups is disrupted?
Certain bonds will not be made which will lead to denaturing the protein (loss of function)
79
4 levels of protein structure
Primary
Secondary
Tertiary
Quaternary
80
Primary structure
Sequence of amino acids linked together in a protein
81
Secondary structure
Helices and pleated sheets
82
Tertiary structure
Complex folding of the protein chain held together by disulfide bridges, hydrophilic/hydrophobic interactions, and other bonds
83
Quaternary
Multiple protein chains are linked together
84
Nucleotides
Make up nucleic acids
85
Nucleotide structure
Phosphate group-5 carbon sugar-nitrogen containing base
86
Two types of nucleotides
Ribonucleotides (A,G, C, U) found in RNA
| Deoxyribonucleotides (A,G,C,T) found in DNA
87
Two types of nucleic acid polymers
DNA found in chromosomes (carries genetic info needed for protein construction )
RNA (copies of DNA used directly in protein construction)
88
Other nucleotides (diff purposes )
Nucleotides as intracellular messengers
...as energy carriers
...as enzyme assistants
89
Nucleotides as intracellular messengers
Cyclic nucleotides carry chemical signals between molecules
90
Nucleotides as energy carriers
ATP carries energy stored in bonds between phosphate groups
| NAD+ and FAD carry electrons
91
Nucleotides as enzyme assistants
Coenzymes help enzymes promote and guide chemical reactions
92
Anabolic reactions
Building up reaction
| Reactant + reactant -> product
93
Catabolic reactions
Breaking down reaction
| Reactant -> product + product
94
Activation energy
The amount of energy needed to start a reaction
95
What happens when chemical bonds form or break?
Energy is either released if absorbed
96
Do anabolic reactions absorb or release energy ?
Absorbs - needs a constant energy source (endothermic)
| Look at graph in ppt
97
Do catabolic reactions absorb or release energy?
Release- spontaneous reactions (but will need a spark or something to start it)
Exothermic
Look at graph in ppt
98
Where do we get energy needed for absorbing (anabolic) reactions?
Humans- food
| Plants- sunlight
99
Catalyst
Speeds up rate of chemical reaction
| Lowers activation energy
100
Enzymes
Proteins that speed up chemical reactions ( by providing a substance for it to occur on)
101
How are enzymes specific?
Enzymes and substrates (reactants) are made for each other like lock (enzyme) and key (substrate)
102
How are enzymes named?
Named after their function + "ase"
Ex: DNA polymerase
103
Substrate
Reactant
| What the enzyme will change
104
Active site
Place on enzymes where substrates bind
105
Enzyme-substrate complex
When enzyme and substrate binds together
106
Denaturing an enzyme
Changing and enzymes shape
107
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Anything that influences a chemical reaction:
pH
Temperature
Regulatory proteins
Inhibitors
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What affects enzymes?
