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GENBIO 1 > Biomolecules > Flashcards

Biomolecules Flashcards

1
Q

Macromolecules, organic molecules

A

Biomolecules

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2
Q

Types of Biomolecules

A

Carbohydrates, Proteins, Lipids, Nucleic acid

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3
Q

How are biomolecules described

A

according to Function

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4
Q

Single unit, building blocks

A

Monomer

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5
Q

Dehydration synthesis is inverse with

A

Hydrolysis

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6
Q

mixing/cooling of diff biomolecule source, formation of bigger molecules

A

Dehydration synthesis

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7
Q

Breaks down from polymer to monomer

A

Hydrolysis

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8
Q

every angle has carbon

A

Carbohydrates

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9
Q

Monosaccharides

A

monomer of Carbon

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10
Q

Polysaccharides and Oligosaccharides are polymers of

A

Carbo

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11
Q

monomers of ___ are what we use as currency/fuel of energy

A

Carbo

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12
Q

Glucose is an example of

A

Monosaccharides

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13
Q

Combination of 2 monosac, can be found in plants and animals

A

Disaccharides

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14
Q

Disaccharides example

A

Lactose, Sucrose

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15
Q

Example of Polysaccharides

A

Cellulose, Glycogen, Starch

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16
Q

Functions of Carbohydrates

A

Energy source, strengthens

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17
Q

dont have any particular monomer

A

Lipids

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18
Q

Components of Lipids

A

Triglycerides

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19
Q

Triglyceride is composed of

A

Glycerol and 3 fatty acids

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20
Q

glycerol+phosphate group+2 fatty acids

A

Phospholipids

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21
Q

lipid bilayer of membranes

A

Phospholipid

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22
Q

Head of phospholipid

A

Hydrophilic

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23
Q

Fats of Phospholipid

A

Hydrophobic

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24
Q

unique, four fused rings attached to each other

A

Sterols

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25
Q

1 pentose rings, 5 carbons

A

Sterols

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26
Q

Component of cell membranes

A

Cholesterol

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27
Q

can be found in food sources, enzymes

A

Proteins

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28
Q

catalyze chem reaction and protect against disease

A

Proteins

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29
Q

store amino acids, transport substances, receive signal, provide structural support

A

Proteins

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30
Q

currency of energy in ATP

A

Nucleic Acid

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31
Q

Sugar=deoxyribose, Nitro based=CGAT

A

DNA

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32
Q

Sugar=ribose, Nitro bases=CGAU

A

RNA

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33
Q

store heridetary into

A

Nucleic acid

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34
Q

provides energy

A

Carbohydrates

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35
Q

Carbon, Hydrogen, Oxy

A

Carb

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36
Q

2C:1H 2H:1O

A

Carb

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37
Q

molecule that mirrors each other

A

Isomers

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38
Q

molecule that mirrors each other

A

Isomer

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39
Q

-ose

A

Sugar and monomer

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40
Q

Mild sweet flavor, always present in sugar, basic unit to produce ATO

A

Glucose

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41
Q

essential energy source, blood sugar

A

Glucose

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42
Q

hardly tastes sweet, attached to another sygar which is glucose, dairy

A

Galactose

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43
Q

Found in Fruits and honey, sweetest

A

Fructose

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44
Q

based on no. of carbons, position of carbonyl group

A

Classification and Naming of sugar

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45
Q

3C

A

triose

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46
Q

5C

A

Pentose

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47
Q

6C

A

Hexose

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48
Q

end

A

aldoses

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49
Q

within

A

ketoses

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50
Q

Plants always have

A

Ketone

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51
Q

Disaccharides contain 2 mono

A

-glucose is always present

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52
Q

Glucose+Fructose

A

Sucrose

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53
Q

Glucose+Glucose

A

Maltose

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54
Q

Glucose + Galactose

A

Lactose

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55
Q

tastes sweet, brown white or powdered

A

Sucrose

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56
Q

Grape wine

A

Sucrose

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57
Q

produced when starch breakd down

A

Maltose

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58
Q

Milo, Beer

A

Maltose

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59
Q

main carbo in milk, came from animals

A

Lactose

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60
Q

short chains, can interact with other molecule

A

Oligosaccharides

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61
Q

long chains, energy storage, structural support

A

Polysaccharides

62
Q

Oligosaccharides has 2

A

or more sugars

63
Q

can stand alone

A

Polysaccharides

64
Q

plants, polymer of glucose monomer

A

Starch

65
Q

energy source, animal sources, structural support

A

Glycogen

66
Q

mahor component if toygh walls,fivers

A

Cellulose

67
Q

cell walls, crab and shrimp

A

Chitin

68
Q

3 groups of lipids

A

Fats, Phospholipids, Steroids

69
Q

has glycerol head and three fatty acids

A

Fats

70
Q

Triglycerides are found in

A

Fats

71
Q

2 types of fats

A

Satureated. Unsaturated

72
Q

long straight chain, mostly animal fats. solid at room temp

A

Satyrated

73
Q

plaque deposits

A

Saturated fats

74
Q

coming from plants and fish, liquid at room temp, presence if double bonds

A

Unsatyrated

75
Q

amino acids

A

Proteins

76
Q

3 groups of proteins

A

amino acid, carboxylic acidbgroup, R group

77
Q

2H:1N

A

Amino acid group

78
Q

C=O-OH

A

Carboxylic acid group

79
Q

R group

A

R side chain

80
Q

Proteins can only function if they are in their

A

Tertiary ajd Quarternary Structute

81
Q

8 types of protein uses

A

Enzymatic, Defensive, Hormonal, Receptor, Storage, Transport, Contractive and Motor, Structural

82
Q

selective accelaeration of chem reactions, ends with -ase

A

Enzymatic Proteins

83
Q

protection against diseases, antibodies

A

Defensive proteins

84
Q

coordination of an organisms activity, ex insulin

A

Hormonal proteins

85
Q

Response of cell to chemical stimuli, built into the membrane of a nerve cell

A

Receptor proteins

86
Q

storage of amino acids

A

Storage proteins

87
Q

the protein of milk, major source of amino acids for baby mammals

A

Casein

88
Q

Highest yileld of protein

A

Low fat milk

89
Q

Plants have storage proteins in their

A

Seeds

90
Q

transport of substances

A

Transport proteins

91
Q

iron-containing protein of vertebrate

A

Transport proteins

92
Q

to enter the cell, the substance should enter the

A

transport proteins

93
Q

movement

A

Contractile and Motor proteins

94
Q

responsible for contraction of muscles

A

Actin and Myosin

95
Q

support

A

Structural proteins

96
Q

Keratin and Collagen

A

Structural proteins

97
Q

Different structures of Proteins

A

Primary, Secondary, Tertiary, Quarternary

98
Q

sequence of chains of amino acids, linear

A

Primary

99
Q

local folding, has angle

A

Secondary protein

100
Q

two types of helix

A

alpha helix and beta-pleated sheet

101
Q

3d folding partern due to chain interaction

A

Teriqry

102
Q

more than one amino acid chain

A

Quarternary

103
Q

amino acid sequence is important in DNA, translation and transcription

A

Primary structure

104
Q

folding, hydrogen bonds

A

Secondary

105
Q

folding 3d

A

Tertiary

106
Q

Factors (Van deer waals) Tertiary

A

Hydro bonds, Ionic vonds, Disulfide bridges

107
Q

Weak

A

Hydro bonds

108
Q

posi and nega charge

A

Ionic bonds

109
Q

sulfur

A

Disulfide bridges

110
Q

Hydrophobic interactions

A

Van deer waals interaction

111
Q

More than 1 polypeptide chain bonds together, protein is now functional

A

Quarternary structure

112
Q

Hemoglobin has how many bonds

A

4

113
Q

Collagen has how many bonds

A

3

114
Q

Protein folding

A

gains function

115
Q

protein unfolding

A

loses function

116
Q

Denaturation

A

Temp, PH, sanity

117
Q

changes a physical characteristic

A

Temp change

118
Q

Myosin & actin and hemoglobin

A

Proteins in meat

119
Q

Steak well done loses

A

hemoglobin

120
Q

pH level of kinilaw

A

acidic

121
Q

Denaturation

A

rebond (denatures pH level), hair are dead cells

122
Q

mobiner of nucleic acid

A

Nucleotide

123
Q

purine

A

two nitro bases

124
Q

Deoxyribose vs Ribose

A

Deoxyribose loxes oxygen

125
Q

Nucleic acid are anti parallel

A

5’ prime, 3 ‘ - 3’, 5’

126
Q

caused by nitrogenous bases, weak and can be broken down by helicase, microRNA or mRNA

A

anti parallel structure

127
Q

Deal with data resulting from sequencing many genomes

A

Bioinformation

128
Q

large sets of genes when comparing whole genomes are called

A

Genomics

129
Q

similar analysis of large sets of proteins

A

proemics

130
Q

alignment of amino acid sequences of B-globun

A

VHLTPEEKSA

131
Q

non polar and insoluble in water

A

Hydrocarbons

132
Q

three fatty acids and one glycerol molecule

A

Triglycerides

133
Q

lipid with double bonds

A

unsaturated

134
Q

solid at room temp

A

Saturated

135
Q

Head pointing towards water

A

Tails up

136
Q

Cholesterol is common in

A

Animals

137
Q

determined by sequence of amino acids

A

Primary structure

138
Q

Hydrogen bonds form helix shape

A

Secondary

139
Q

hydrophilic parts would face wayer and hydrophobic turn inward

A

Tertiary

140
Q

two pairs if similar polypeptides, eacy contains oxygen carrying heme mokecule

A

Hemoglobin molecule

141
Q

quarternary structure

A

has more than one polypeptide chain

142
Q

Formation of chem bonds

A

electrons

143
Q

fewer neutrons

A

isotopes

144
Q

Glucose is a

A

monosaccharide

145
Q

posituve and negative charge of an oxy and nitro

A

Hydrogen bonds

146
Q

60% of water

A

Blood

147
Q

polar molecules are

A

hydrophilic

148
Q

loss of bio function

A

denaturation

149
Q

A and G

A

Purine

150
Q

C and T

A

Pyrimidines

GENBIO 1 (2 decks)

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