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Biomolecules Flashcards

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1
Q

What are the primary functions of carbonhydrates ?

A

They are for fuel/energy (immediate and stored) and for structure (especially in plants).

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2
Q

What are polymers ?

A

Linked monomers

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3
Q

How is formed a polymer ( polymerization)?

A

By the removal of water. It is called a dehydration reaction or a condensation reaction.

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4
Q

How are polymers broken down ( depolymerization)?

A

By adding water, which is called hydrolysis

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5
Q

How is called a carbonhydrate monomer ?

A

A monosaccharide

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6
Q

How is called a carbonhydrate polymer ?

A

A polysaccharide

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7
Q

What is the formula for a monosaccharide ?

A

CxH2xOx

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8
Q

What is the formula for a disaccharide ?

A

CxH2(x-1)O(x-1)

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9
Q

How can carbonhydrates be drawn ?

A

As a long vertical chain (fisher projection) or as a ring.

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10
Q

How is called the link between two monosaccharides ?

A

A glycosidic link/bond

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11
Q

If the OH group on the first carbon sticks upwards, what is its orientation ?

A

It is beta

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12
Q

If the OH group on the fisrt carbon sticks downwards, what is its orientation ?

A

It is alpha

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13
Q

How is called the glycosidic bond in maltose (2 glucose monomers) ?

A

An alpha 1-4 bond/linkage

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14
Q

How is called the glycosidic bond in lactose (1 glucose and 1 beta-galctose) ?

A

A beta 1-4 bond /linkage

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15
Q

How is called the glycosidic bond in sucrose (1 alpha glucose, 1 fructose) ?

A

An alpha 1-2 bond/linkage

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16
Q

Of what is made glycogen ?

A

it is composed of glucose connected by alpha 1-4 bonds and with many branching points of alpha 1-6 bonds. It is found in animals and is stored within liver and muscles.

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17
Q

What is glycogen function ?

A

A storage for glucose that can quickly be hydrolysed (used up) thanks to its many branching points.

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18
Q

What is amylopectin ?

A

One of the two polysaccharides that forms starch. It is found in plants. It has the same types of bonds as glycogen but does not have as many branching points.

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19
Q

What is amylopectin function ?

A

Intermediate-“term” glucose storage.

Found in plants and stored as granules within choloroplast

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20
Q

What is amylose ?

A

The second component of starch. It is a continuous chain of glucose with an alpha 1-4 bond. It has no branching points.

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21
Q

What is amylose function ?

A

Long-term storage of glucose

Found in plants and stored as granules within choloroplast

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22
Q

What is cellulose ?

A

It consists of glucose with beta 1-4 bonds. It causes the chains of glucose to form step-like strands.

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23
Q

What is cellulose function ?

A

It is a major component of plant cell wall

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24
Q

What is the primary function of nucleic acids ?

A

To store genetic information.

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25
Q

How is called a nucleic acid monomer ?

A

A nucleotide

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26
Q

How is called the bond between two nucleotides ?

A

A phosphodiester bond

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27
Q

Of what is made a nucleotide ?

A

A phosphate group, a pentose sugar and a nitrogenous base.

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28
Q

What are the two possible pentose sugars found in a nucleotide ?

A

Ribose or deoxyribose

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29
Q

What is RNA ?

A

RNA (ribonucleic acid) is a polymer of nucleotides with a ribose pentose sugar.

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30
Q

What is DNA ?

A

DNA (deoxyribonucleic acid) is a polymer of nucleotides with a deoxyribose pentose sugar.

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31
Q

What are the two purines ?

A

Adenine (A) and Guanine (G)

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32
Q

What are the three pyrimidines ?

A

Cytosine (C), Thymine (T) and Uracil (U)

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33
Q

What purines /pyrimidines does DNA have ?

A

A-T and C-G

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34
Q

What purines /pyrimidines does RNA have ?

A

A-U and C-G

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35
Q

How many hydrogen bonds does C and G form ?

A

three

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36
Q

How many hydrogen bonds does A and T/U form ?

A

two

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37
Q

What is base stacking ?

A

The stacking up of the different nitrogenous bases to stabilize each other.

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38
Q

What controls the double-stranded nature of DNA ?

A

Base stacking and hydrogen bonding.

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39
Q

What are characteristics of RNA ?

A

It is usually single-stranded.

It is considered more fragile than DNA.

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40
Q

What are some of the functions that a protein can have ?

A

Accelerate certain chemical reactions (enzymatic)
Protection against disease (defensive )
Storage of amino acids (storage)
Transport of substances (transport)
Coordination of an organism’s activities (hormonal)
Response of cell to chemical stimuli (receptor)
Movement (contractile and motor)
Support (structural)

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41
Q

What determines the protein’s function(s) ?

A

The protein’s structure

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42
Q

How is called the bond between two amino acids ?

A

A peptide bond

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43
Q

How is called a protein’s monomer ?

A

An amino acid or a peptide

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44
Q

Of what is composed an amino acid ?

A

An amino group, an R group side chain and a carboxyl group

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45
Q

How many possible R groups are there for an amino acid ?

A

20 different R groups

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46
Q

What is an hydrophobic (non-polar) side chain ?

A

A side chain that contains only C and H.

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47
Q

What is an hydrophilic (polar) side chain ?

A

A side chain that has an OH, SH or a carbonyl group

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48
Q

What is an acidic side chain ?

A

A side chain capable of donating a proton

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49
Q

What is an basic side chain ?

A

A side chain capable of receiving a proton

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50
Q

What is an amphipathic molecule ?

A

A molecule that has both a polar and a non-polar part.

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51
Q

What are some particularities of glycine ?

A

It has no stereoisomers, unlike the other amino acids.
It is very flexible
It is smaller than the other amino acids.

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52
Q

What are some particularities of proline ?

A

Its side chain actually links with its backbone.

It is extremely rigid.

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53
Q

What is a particularity of an amino acid with an hydrophobic side chain ?

A

It is amphipathic.

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54
Q

Between what is a peptide bond formed ?

A

Between the amino nitrogen of one amino acid and the carboxyl carbon of the next amino acid.

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55
Q

What is the primary protein structure ?

A

The written out list of amino acids that exist in the protein from the N to the C terminal.

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56
Q

What is the secondary protein structure ?

A

The specific folding of the protein. it is determined through the hydrogen bonding interactions between the backbones of the polypeptide chain.

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57
Q

What two types of folds can occur in a protein ?

A

alpha-helices (coiled tubes) and beta pleated sheets (flat “waves”)

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58
Q

What is the tertiary protein structure ?

A

The interactions between the side chains of the amino acids in the protein (such as hydrogen bonding, ionic bonds and disulfide bridges).

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59
Q

What is the quaternary protein structure ?

A

It takes into consideration when more than one polypeptide chain cluster together to form a macromolecule. It is the interaction between those different polypeptide chains that are considered the quaternary structure.

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60
Q

What does an enzymatic protein ?

A

It binds to a specific molecule and changes it (it is a catalyst).

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61
Q

When does protein denaturation happen ?

A

When the interactions that cause protein folding are intefered with.

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62
Q

What can influence whether a protein is in its proper structure or not ?

A

Temperature
pH changes
Salt concentrations
Solvent used

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63
Q

Is denaturation reversible ?

A

Yes, it usually is since the primary structure is intact.

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64
Q

Lipids consist primarily of what moleculels ?

A

Of carbon and hydrogen molecules (hydrocarbons).

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65
Q

What is the general formula of fatty acids ?

A

saturated : CxH2xO2 (no double bonds)

unsaturated : CxH2(x-n)O2 (double bond(s) )

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66
Q

What causes the double bond found in unsaturated fatty acids ?

A

It causes a kink in the hydrocarbon chain.

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67
Q

Of what are composed triglycerides/fats ?

A

Of a glycerol molecule linked to three fatty acids

68
Q

Are triglycerides polar or not ?

A

They are non-polar.

69
Q

Of what are phospholipids composed ?

A

Of two fatty acids, a glycerol attached to a phosphate group and a variable hydrophilic group

70
Q

What are some of the propreties of phospholipids ?

A

They are amphipathic molecules (they have an hydrophilic head and an hydrophobic tail)
When added to water, they assemble into a bilayer
Major component of all cell membranes

71
Q

What is a common feature to all steroids ?

A

A carbon skeleton that consists of 4 fused rings

72
Q

What is one of the propreties of steroids ?

A

They are all amphipathic molecules,

73
Q

What are examples of a steroid ?

A

Cholesterol
Bile acids
Vitamin D
Hormones

74
Q

Monosaccharides vary in what?

A

Location of carbonyl group (ketoses or aldoses)
Number of C in the skeleton (usaully 3, 5 or 6)
Isomers( structural, enantiomers, strereoisomers)

75
Q

What is an anomeric carbon?

A

The carbon on which the carbonyl group is

76
Q

Why is cellulose a stable structural molecule?

A

Few organisms have the enzymes to hydrolyse the beta linkages in cellulose
No caloric value for most animals (insoluble fibers)

77
Q

From where do almost half of our calories come from?

A

From starch

78
Q

What is chitin?

A

A semi-rigid structural polysaccharide (composed of glucose + an appendage containing N -> N-acetyl glucosamine)

79
Q

Where is chitin found?

A

In exoskeleton of arthropods

In fungi cell walls

80
Q

What is the general structure of a fatty acid?

A

A carboxyl group attached to a hydrocarbon chain (usually between 12 to 24 C)

81
Q

Under what from are unsaturated fatty acids found in nature?

A

As cis stereoisomers

82
Q

What are essential fatty acids (EFA) ?

A

Fatty acids that cannot be synthesised in our body (must be obtained from diet)

83
Q

What are eicosanoids ?

A

Molecules made by oxygenation of 20 carbons EFA

Signalling molecules involved in inflammation and as messengers in nervous system

84
Q

Eicosanoids are either what ?

A

omega-3

omega-6

85
Q

What is the difference between omega-3 and omega-6 ?

A

omega-3 are anti-inflammatory

omega-6 are pro-inflammatory

86
Q

What does the balance between w-3 and w-6 in diet affect?

A

Triglyceride level
Blood pressure
Cardiovascular disease
Inflammatory disorders

87
Q

What drugs stop the synthesis of eicosanoids?

A

Aspirin

Ibuprofen

88
Q

What are classes of eicosanoids ?

A

Prostaglandins
Leukotriene
Thromboxane

89
Q

In what organisms are saturated fats the most common?

A

In terrestrial animals

90
Q

How are saturated fats produced?

A

By the hydrogenation of unsaturated fats

91
Q

In what state are saturated fats at room temperature?

A

They are solid

92
Q

In what state are unsaturated fats at room temperature?

A

They are liquid

93
Q

In what organisms are unsaturated fats the most common?

A

Fish

Plants

94
Q

What are the chemical propreties of fats?

A

Non-polar
Neutral
Hydrophobic

95
Q

What are the main functions of fats?

A

Long term energy storage

96
Q

What are the functions of adipose tissues?

A

Store fats (in mammals)
Cushion vital organs
Insulate the body

97
Q

What are the particularities of phospholipids with unsaturated fatty acids?

A

They have a lower freezing point

They tend to aggregate less

98
Q

What are the functions of cholesterol?

A

Temperature buffer

Regulates membrane fluidity

99
Q

Where are bile acids produced?

A

In the liver of mammals

100
Q

What is the main function of bile acids?

A

Digest fats (fats aren’t water soluble)

101
Q

Where can vitamin D be found?

A

Produced when skin exposed to sunlight

Found in diet

102
Q

What are some of the roles of vitamin D ?

A

It promotes the absorption and metabolism of Ca and P
It is involved in cancer prevention
Deficit linked to multiple sclerosis

103
Q

How are waxes defined?

A

As a substance similar in composition and physical propreties to beeswax

104
Q

What is the biological importance of waxes?

A

Plant cuticule
Insect waxes (ex: beeswax)
Water proofing of feathers (in birds)
Found on skin surface and in ears (earwax)

105
Q

What roles do waxes play in some marine organisms?

A

Energy source
Insulation
Buoyancy control (flotability)
Echolocation

106
Q

What do sphingolipids contain?

A

Sphingosine

107
Q

What are the functions of sphingolipids?

A

Protect cell surface by forming stable structure part of the outer leaflet of phospholipid bilayer
Role in signal transmission (form lipid rafts)
Involved in cell recognition

108
Q

What are glycolipids?

A

Lipids attached to carbonhydrates

109
Q

What are the functions of glycolipids?

A

Recognition sites/ chemical signature of cells

Contribute to cell attachment to form tissues

110
Q

Approximatively what percentage of the dry mass of most cells consists of proteins?

A

> 50%

111
Q

What are proteins?

A

Polymers built from the same set of 20 amino acids

112
Q

Why do amino acids differ in their propreties?

A

Because of their different side chains

113
Q

What are zwitterions?

A

Amino acids that carry both a + and a - charge

114
Q

What are a few propreties of zwitterions?

A

Form at isoelectric point
Net charge is of 0
Polar
Hydrophilic

115
Q

What is the isoelectric point (pI)?

A

The pH at which an amino acid/protein has a net electric charge of 0

116
Q

What charge will a protein have if the pH is lower than the isoelectric point?

A

A positive charge

117
Q

What charge will a protein have if the pH is higher than the isoelectric point?

A

A negative charge

118
Q

What happens to proteins at the isoelectric point?

A

They aggregate and precipitate out of the solution

119
Q

In order from the weakest to the strongest, name the types of interactions between the R groups of the amino acids in a protein

A 
Van der Waals
Covalent bond (hydrophobic interactions)
H-bonds
Ionic bonds
Disulfide bridges
120
Q

Which amino acid allows the formation of disulfide bridges?

A

Cysteine

121
Q

What are examples of proteins with a quaternary structure?

A

Hemoglobin

Collagen

122
Q

What can be associated to several diseases?

A

The aggregation of misfolded protein

123
Q

To what type of diseases are misfolded proteins associated to ?

A

Prion-related illness
Amyloid-related illness
Intracytoplasmic aggregation disease

124
Q

What do prion diseases affect?

A

The structure of the brain

Other neural tissues

125
Q

What is an example of prion-related disease?

A

BSE ( mad cow disease)

CJD ( Creutzfeldt-Jakob disease -> in humains)

126
Q

What is an example of amyloid-related disease?

A

Alzheimer’s

127
Q

What is the leading hypothesis as to what causes Alzheimer’s ?

A

By the deposits of amyloid-β (Aβ) protein

It accumulates in the brain and contributes to nerve cell damage

128
Q

What is an example of intracytoplasmic aggregation disease?

A

Parkinson’s disease

129
Q

What characterizes Parkinson’s disease?

A

The death of brain cells

The accumulation of α-synuclein protein into the Lewy bodies in neurons

130
Q

What structures are altered when protein denaturation happens?

A

The secondary and tertiary structures

131
Q

What can cause protein denaturation?

A

Heat
Alcohol
Mercurochrome

132
Q

How many grams of protein per kg lean body weight are there in adults?

A

At least 0.8g

133
Q

What are the functions of dietary proteins?

A

Source of essential amino acids (EAA)
Source of energy
Excess converted to sugars and fatty acids

134
Q

What is a common cause of health problems and mortality in developing countries?

A

Protein deficiency

135
Q

What is a characteristic of essential amino acids (EAA) ?

A

They can’t be synthesized by the organism (so must obtained by diet)

136
Q

What is the most important source of animal proteins for humains?

A

Fish

137
Q

What determines the amino acid sequence of a certain protein?

A

Genes

138
Q

Genes are sequences of what?

A

Of DNA

139
Q

What is a nucleoside?

A

A nucleotide without the phosphate group

140
Q

How are adjacent nucleotides joined together?

A

By a covalent bond between the -OH group on the 3 C of a nucleotide and the phosphate on the 5 C of the next one

The phosphate group and the pentode sugar form the backbone

141
Q

What did Chargaff found?

A

That DNA was species specific

That %A = %T and %G = %C

142
Q

What did Franklin and Wilkins discover?

A

That DNA was formed of two antiparallel sugar-phosphate backbones, with the nitrogenous bases paired in the molecule’s interior

143
Q

What did Watson and Crick do?

A

They build models of a double helix for DNA

144
Q

What are vitamins ?

A

Organic compounds required by an organism as a vital nutrient (must be obtained from diet)

145
Q

Based on what are vitamins grouped?

A

Based on their biological activity

146
Q

What is the function of vitamin B ?

A

Important roles in cell metabolism and respiration

147
Q

What are examples of vitamin B ?

A

Thiamine
Riboflavin
Niacin

148
Q

In what is vitamin C (ascorbic acid) involved ?

A

In the functionning of immune cells

149
Q

What are characteristics of vitamin C

A

It is a cofactor (electron donor) for at least 8 enzymes

It is an antioxidant (reducing agent)

150
Q

To what can lead a deficiency in vitamin C ?

A

To scurvy

To unstable collagen

151
Q

What classes of life’ s organic molecules contain polymers ?

A

Carbohydrates
Proteins
Nucleic acids

152
Q

What are the enantiomers of glucose and their function?

A

D-glucose (dextrose) : biologically active

L-glucose: not metabolized by cells in glycolysis

153
Q

What condition is needed for a saccharide to be a reducing sugar?

A

It must have an available anomeric carbon

154
Q

By what is the structure and function of a polysaccharide determined?

A

By the type of monosaccharide it is made of

By the position of the glycosidic linkages

155
Q

What is the most abundant large organic compound on Earth?

A

Cellulose

156
Q

What role does essential fatty acids play ?

A

Development of nervous system
Lowers inflammation
Deficiency associated with depression, schizophrenia, heart diseases and cancer

157
Q

Where are fats stored?

A

In adipose cells

158
Q

Triglycerides are used to make soap by what process?

A

By saponification

159
Q

What happens when phospholipids are added to water?

A

Bilayer formation with hydrophobic tails pointing toward the interior

160
Q

What is the main role of phospholipids?

A

Major component of cell membrane

161
Q

Where are bile acids produced?

A

In the liver of mammals

162
Q

What is the function of chaperonins?

A

They assist in protein folding

163
Q

How does prion diseases propagate?

A

They induce properly folded proteins to misfold and convert to prion
The prions then aggregated (amyloid fold formation)
Aggregates disrupt normal tissue structure

164
Q

What was done to control BSE ?

A

Ban on feeding cattle with meat and bone meal
Import control
Surveillance measures

165
Q

What is a conjugated protein?

A

A protein attached to non-amino groups (prosthetic group)

166
Q

What are examples of conjugated proteins ?

A

Lipoproteins
Hemoglobin (contains heme group)
Cytochromes ( contains heme group)

167
Q

What triggers allergic reactions to certain foods?

A

Some proteins

Biology (8 decks)

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