Biomolecules Flashcards
(150 cards)
1
Q
Macromolecules, organic molecules
A
Biomolecules
2
Q
Types of Biomolecules
A
Carbohydrates, Proteins, Lipids, Nucleic acid
3
Q
How are biomolecules described
A
according to Function
4
Q
Single unit, building blocks
A
Monomer
5
Q
Dehydration synthesis is inverse with
A
Hydrolysis
6
Q
mixing/cooling of diff biomolecule source, formation of bigger molecules
A
Dehydration synthesis
7
Q
Breaks down from polymer to monomer
A
Hydrolysis
8
Q
every angle has carbon
A
Carbohydrates
9
Q
Monosaccharides
A
monomer of Carbon
10
Q
Polysaccharides and Oligosaccharides are polymers of
A
Carbo
11
Q
monomers of ___ are what we use as currency/fuel of energy
A
Carbo
12
Q
Glucose is an example of
A
Monosaccharides
13
Q
Combination of 2 monosac, can be found in plants and animals
A
Disaccharides
14
Q
Disaccharides example
A
Lactose, Sucrose
15
Q
Example of Polysaccharides
A
Cellulose, Glycogen, Starch
16
Q
Functions of Carbohydrates
A
Energy source, strengthens
17
Q
dont have any particular monomer
A
Lipids
18
Q
Components of Lipids
A
Triglycerides
19
Q
Triglyceride is composed of
A
Glycerol and 3 fatty acids
20
Q
glycerol+phosphate group+2 fatty acids
A
Phospholipids
21
Q
lipid bilayer of membranes
A
Phospholipid
22
Q
Head of phospholipid
A
Hydrophilic
23
Q
Fats of Phospholipid
A
Hydrophobic
24
Q
unique, four fused rings attached to each other
A
Sterols
25
1 pentose rings, 5 carbons
Sterols
26
Component of cell membranes
Cholesterol
27
can be found in food sources, enzymes
Proteins
28
catalyze chem reaction and protect against disease
Proteins
29
store amino acids, transport substances, receive signal, provide structural support
Proteins
30
currency of energy in ATP
Nucleic Acid
31
Sugar=deoxyribose, Nitro based=CGAT
DNA
32
Sugar=ribose, Nitro bases=CGAU
RNA
33
store heridetary into
Nucleic acid
34
provides energy
Carbohydrates
35
Carbon, Hydrogen, Oxy
Carb
36
2C:1H 2H:1O
Carb
37
molecule that mirrors each other
Isomers
38
molecule that mirrors each other
Isomer
39
-ose
Sugar and monomer
40
Mild sweet flavor, always present in sugar, basic unit to produce ATO
Glucose
41
essential energy source, blood sugar
Glucose
42
hardly tastes sweet, attached to another sygar which is glucose, dairy
Galactose
43
Found in Fruits and honey, sweetest
Fructose
44
based on no. of carbons, position of carbonyl group
Classification and Naming of sugar
45
3C
triose
46
5C
Pentose
47
6C
Hexose
48
end
aldoses
49
within
ketoses
50
Plants always have
Ketone
51
Disaccharides contain 2 mono
-glucose is always present
52
Glucose+Fructose
Sucrose
53
Glucose+Glucose
Maltose
54
Glucose + Galactose
Lactose
55
tastes sweet, brown white or powdered
Sucrose
56
Grape wine
Sucrose
57
produced when starch breakd down
Maltose
58
Milo, Beer
Maltose
59
main carbo in milk, came from animals
Lactose
60
short chains, can interact with other molecule
Oligosaccharides
61
long chains, energy storage, structural support
Polysaccharides
62
Oligosaccharides has 2
or more sugars
63
can stand alone
Polysaccharides
64
plants, polymer of glucose monomer
Starch
65
energy source, animal sources, structural support
Glycogen
66
mahor component if toygh walls,fivers
Cellulose
67
cell walls, crab and shrimp
Chitin
68
3 groups of lipids
Fats, Phospholipids, Steroids
69
has glycerol head and three fatty acids
Fats
70
Triglycerides are found in
Fats
71
2 types of fats
Satureated. Unsaturated
72
long straight chain, mostly animal fats. solid at room temp
Satyrated
73
plaque deposits
Saturated fats
74
coming from plants and fish, liquid at room temp, presence if double bonds
Unsatyrated
75
amino acids
Proteins
76
3 groups of proteins
amino acid, carboxylic acidbgroup, R group
77
2H:1N
Amino acid group
78
C=O-OH
Carboxylic acid group
79
R group
R side chain
80
Proteins can only function if they are in their
Tertiary ajd Quarternary Structute
81
8 types of protein uses
Enzymatic, Defensive, Hormonal, Receptor, Storage, Transport, Contractive and Motor, Structural
82
selective accelaeration of chem reactions, ends with -ase
Enzymatic Proteins
83
protection against diseases, antibodies
Defensive proteins
84
coordination of an organisms activity, ex insulin
Hormonal proteins
85
Response of cell to chemical stimuli, built into the membrane of a nerve cell
Receptor proteins
86
storage of amino acids
Storage proteins
87
the protein of milk, major source of amino acids for baby mammals
Casein
88
Highest yileld of protein
Low fat milk
89
Plants have storage proteins in their
Seeds
90
transport of substances
Transport proteins
91
iron-containing protein of vertebrate
Transport proteins
92
to enter the cell, the substance should enter the
transport proteins
93
movement
Contractile and Motor proteins
94
responsible for contraction of muscles
Actin and Myosin
95
support
Structural proteins
96
Keratin and Collagen
Structural proteins
97
Different structures of Proteins
Primary, Secondary, Tertiary, Quarternary
98
sequence of chains of amino acids, linear
Primary
99
local folding, has angle
Secondary protein
100
two types of helix
alpha helix and beta-pleated sheet
101
3d folding partern due to chain interaction
Teriqry
102
more than one amino acid chain
Quarternary
103
amino acid sequence is important in DNA, translation and transcription
Primary structure
104
folding, hydrogen bonds
Secondary
105
folding 3d
Tertiary
106
Factors (Van deer waals) Tertiary
Hydro bonds, Ionic vonds, Disulfide bridges
107
Weak
Hydro bonds
108
posi and nega charge
Ionic bonds
109
sulfur
Disulfide bridges
110
Hydrophobic interactions
Van deer waals interaction
111
More than 1 polypeptide chain bonds together, protein is now functional
Quarternary structure
112
Hemoglobin has how many bonds
4
113
Collagen has how many bonds
3
114
Protein folding
gains function
115
protein unfolding
loses function
116
Denaturation
Temp, PH, sanity
117
changes a physical characteristic
Temp change
118
Myosin & actin and hemoglobin
Proteins in meat
119
Steak well done loses
hemoglobin
120
pH level of kinilaw
acidic
121
Denaturation
rebond (denatures pH level), hair are dead cells
122
mobiner of nucleic acid
Nucleotide
123
purine
two nitro bases
124
Deoxyribose vs Ribose
Deoxyribose loxes oxygen
125
Nucleic acid are anti parallel
5’ prime, 3 ‘ - 3’, 5’
126
caused by nitrogenous bases, weak and can be broken down by helicase, microRNA or mRNA
anti parallel structure
127
Deal with data resulting from sequencing many genomes
Bioinformation
128
large sets of genes when comparing whole genomes are called
Genomics
129
similar analysis of large sets of proteins
proemics
130
alignment of amino acid sequences of B-globun
VHLTPEEKSA
131
non polar and insoluble in water
Hydrocarbons
132
three fatty acids and one glycerol molecule
Triglycerides
133
lipid with double bonds
unsaturated
134
solid at room temp
Saturated
135
Head pointing towards water
Tails up
136
Cholesterol is common in
Animals
137
determined by sequence of amino acids
Primary structure
138
Hydrogen bonds form helix shape
Secondary
139
hydrophilic parts would face wayer and hydrophobic turn inward
Tertiary
140
two pairs if similar polypeptides, eacy contains oxygen carrying heme mokecule
Hemoglobin molecule
141
quarternary structure
has more than one polypeptide chain
142
Formation of chem bonds
electrons
143
fewer neutrons
isotopes
144
Glucose is a
monosaccharide
145
posituve and negative charge of an oxy and nitro
Hydrogen bonds
146
60% of water
Blood
147
polar molecules are
hydrophilic
148
loss of bio function
denaturation
149
A and G
Purine
150
C and T
Pyrimidines
