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IB Biology > B1 > Flashcards

B1 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Macromolecule

A

Very large molecule made up for many repeating sub-units

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2
Q

Monomers

A

Repeating small units that make up macromolecules

Smallest unit still classified as that molecule type

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3
Q

Condensation reaction

A

Reaction involving the formation of a covalent bond between two monomers to form polymers.

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4
Q

What is the role of water in a condensation reaction?

A

Remove hydroxyl (OH) from one monomer and hydrogen (H) from the other to make them reactive. Together, they combine to make H2O as a waste product.

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5
Q

Hydrolysis

A

Reaction that breaks bonds of the polymer to split into many monomers.

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6
Q

Role of water in hydrolysis

A

Water molecule is split. H is added to one monomer, and OH to the other. This stabilises monomers to prevent rebonding. Therefore, water is need (reactant)

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7
Q

What features of carbon make it able to form many unique compounds?

A

4 valence electrons in outer shell -> can form 4 covalent bonds (double or single). Very effective at forming bonds with other atoms
Can form long chains and rings

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8
Q

Monomer for carbohydrate

A

Monosaccharide

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9
Q

Monomer for lipids

A

Fatty acids (plus a glycerol and/or phosphate group)

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10
Q

Monomers for proteins

A

Amino acids

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11
Q

Monomers for nucleic acids

A

Nucleotides

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12
Q

Processes in body that use condensation reactions

A

Building body tissue
Protein synthesis
DNA replication and transcription
Glycogen and starch formation

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13
Q

Why is water produced when condensation reactions occur?

A

During these reactions, stable monomers must become reactive (by removing H from one monomer and OH from the other). H and OH combine to make water

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14
Q

What are examples of processes in your body that use hydrolysis reactions?

A

Anytime larger macromolecules are broken down to use the building blocks
e.g. digestion

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15
Q

What role does water play in hydrolysis reactions?

A

After breaking bonds in polymer, monomers are reactive. To prevent reconnection, H2O is split. H goes to one monomer, and OH to the other. This makes the monomers stable and non-reactive

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16
Q

Polymerisation of monosaccharides

A

OH is removed from C1 of one monosaccharide.
H is removed from C4 of one monosaccharide.
This generates a disaccharide, which will become a polysaccharide if the polymerisation continues. The bond is called a 1-4 glycosidic linkage. H2O is also produced

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17
Q

What is the name for the bond between monosaccharides?

A

1-4 glycosidic linkage

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18
Q

Polymerisation of fatty acids and glycerol

A

OH is removed from glycerol. H is removed from the fatty acid. This forms a bond between the C of the glycerol and the O of the fatty acid. The bond is called an ester linkage/bond. 3 H2O is also produced. Whole new molecule is a triglyceride

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19
Q

Name of the bond between fatty acids and glycerol

A

Ester linkage/bond

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20
Q

Name of molecule formed by polymerisation of fatty acids and glycerol

A

Triglyceride

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21
Q

Polymerisation of amino acids

A

OH off carboxyl end. H off amine group. Leads to a peptide bond between C of carboxyl group and N of amine group. H2O is also produced.
Molecule is called a dipeptide, and will become a polypeptide is continued

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22
Q

Name of bond between amino acids

A

Peptide bond

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23
Q

Polymerisation of nucleotide

A

H off C3 sugar
OH off phosphate group.
Leads to a phosphodiester bond, and water. Molecule is either DNA backbone (replication) for mRNA (transcription)

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24
Q

Name of bond between nucleotides

A

Phosphodiester bond

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25
Q

Monosaccharide

A

Monomer of all carbohydrates.

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26
Q

Traits of monosaccharides

A

5 or 6 carbons. Form rings in aqueous solutions

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27
Q

Examples of monosaccharides

A

Ribose, deoxyribose, glucose

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28
Q

Polysaccharide

A

When many monosaccharides are chemically bonded together (AKA complex carbohydrates). Can be broken into monosaccharides to provide energy or perform structure functions in cells

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29
Q

Cellulose

A

Polysaccharide that makes up cell walls in plants

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30
Q

Glycoproteins

A

Carbohydrate chemically bonded to a protein. Found in cell membrane where carbohydrate chain is anchored to a member protein

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31
Q

Pentose vs hexose sugar

A

Pentose monosaccharides: contains 5 carbons in carbon backbone C5H10O6

Hexose monosaccharide: contains 6 carbons in carbon backbone. C6H12O6

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32
Q

What makes glucose a polar molecule?

A

Its 5 hydroxyl groups, which exist in a polar covalent bond.

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33
Q

What type of molecule is glucose?

A

Monosaccharide

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34
Q

What is the charge distribution for a hydroxyl group?

A

H is slightly positive. O is slightly negative

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35
Q

Formula for glucose

A

C6H12O6

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36
Q

Alpha glucose v.s. beta glucose

A

At C1, alpha glucose has the H above the hexose ring and the OH below.

For beta glucose, the OH is above the hexose ring, and H is below it.

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37
Q

Structure of glucose

A

Six carbon. Hexose-ring

Order
O
C1 (H above, OH below for alpha. OH above, H below for beta)
C2 (H above, OH below)
C3 (Oh above, H below)
C4 (H above, OH below)
C5 (CH2OH branches off. C6 is this C)

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38
Q

Properties of glucose and how determined

A

Molecular stability (due to covalent bonds)

High solubility in water (due to polarity)

Easily transportable (due to solubility)

Yields high energy (ATP) when oxidised due to covalency

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39
Q

Examples of polysaccharides

A

Amylose
Amylopectin
Glycogen
Cellulose

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40
Q

Amylose strucutre

A

Straight chain of alpha glucose (i.e. long chain of glucose molecules). Only 1-4 linkages. Helix shape overall

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41
Q

Function of amylose

A

20% of plant starch; therefore, long-term storage in plants.

Storage function is facilitated by being able to be compact. Bonds between glucose molecules are easily broken by hydrolysis to free monosaccharides for cellular respiratoin

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42
Q

Amylopectin structure

A

Branched chain of alpha glucose. Made up of 1-4 linkages and some 1-6 linkages.

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43
Q

Function of amylopectin

A

80% of plant starch; therefore, long-term storage in plants.

Storage function is facilitated by being able to be compact. Bonds between glucose molecules are easily broken by hydrolysis to free monosaccharides for cellular respiratoin

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44
Q

Structure of glycogen

A

Highly branched chain of glucose. 1-4 linkages and lots of 1-6 linkages

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45
Q

Function of glycogen

A

Short-term energy storage for animals. Humans store in the liver

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46
Q

Why is glycogen ideal structurally for energy storage?

A

Can form coils/chains therefore compact storage molecules. Bonds between glucose molecuels can easily be broken by hydrolysis

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47
Q

Purpose of bonds between glucose in starch and glycogen being broken

A

To free monosaccharides for cellular respiration

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48
Q

Cellulose structure

A

Straight chain of alternating beta glucose (some flipped on x-axis). Only 1-4 linkages. Hydrogen bonds between long fibres

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49
Q

Function of cellulose

A

Structural component and strong fibes. Used for plant cell walls.

(Humans don’t break it down -> fibre)

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50
Q

What is a glycoprotein?

A

Carbohydrate chain attached to a cell membrane protein

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51
Q

Role of glycoproteins

A

Used for cell identification

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52
Q

Glycoproteins and ABO blood type

A

Glycogen proteins detect antigens for the blood types.
E.g.
Type A glycoproteins detect A antigens
Type B glycoproteins detect B antigen
Type AB glycoproteins detect A and B antigens
Type O glycoproteins detect neither

53
Q

Phospholipids

A

Modified triglyceride that contains a glycerol, two fatty acids and a phosphate group (formed by a condensation reaction)

54
Q

Adipose tissue

A

Composed of specialised cells (adipocytes) that store triglycerides as stored energy. Makes up body fat

55
Q

Amphipathic

A

Molecule with body hydrophobic and hydrophilic regions

56
Q

Endotherms

A

Organisms that maintain a steady internal temperature regardless of changes in external temperature

57
Q

How do non-polar covalent bonds impact the characteristics of lipids?

A

Lipids are defined by long fatty acid chains that are made up of carbon and hydrogen (form non-polar covalent bonds). Therefore, lipids are non-polar and do not dissolve in water.

58
Q

Types of lipid

A

triglycerides
phospholipid
steroids

59
Q

Structure of triglyceride

A

Glycerol with three fatty acids. Can either be saturated or unsaturated

60
Q

Function of triglycerides

A

Form adipose tissues. Stores triglycerides in cells

61
Q

Why are triglycerides an effective molecule for long-term energy storage?

A

Stable but release lots of energy when broken

Hydrophobic (does not pull water)

Poor heat conductors (insulation)

62
Q

Structure of phospholipid

A

Glycerol
2 x fatty acid
Phosphate

Can either be saturated or unsaturated

63
Q

Function of phospholipid

A

Form bilayer of cells and organelle membranes

(amphipathic)

64
Q

Structure of steroids

A

Form C-H rings instead of chains from cholestrol

65
Q

Function of steroids

A

Make up steroid hormone messages.

Lipid-based = hydrophobic, can pass through all membrane to enter cells

66
Q

Regions of phospholipid

A

Polar head
Non-polar fatty acid tails

67
Q

How does the phosphate group become a part of the phospholipid?

A

Condensation reaction. OH removed from glycerol.
H removed from phosphate group. Form esther linkage

68
Q

Types of fatty acids

A

Saturated
Monounsaturated
Polyunsaturated

69
Q

Definition of saturated fatty acid

A

Only single bonds between carbons (straighter shape)

70
Q

Properties of saturated fatty acids

A

Highly compressible -> efficient storage in adipose tissue

High MP due to stability -> solid fats

71
Q

Examples of saturated fats

A

Form adipose tissue, fatty meats and butter

72
Q

Monounsaturated fatty acid

A

One double bond ebtween carbons

73
Q

Properties of monounsaturated fatty acids

A

Less dense, more spread out.
Ideal for cell membranes
Lower MP generally, so liquid at room temperature

74
Q

Examples of monounsaturated fatty acids

A

Come from plants. Used for waterproof covering in plants
Olive oil

75
Q

Polyunsaturated fatty acids

A

More than one double bond between Carbons

76
Q

Properties of polyunsaturated fatty acids

A

Even lower melting point

77
Q

Polyunsaturated fatty acids examples

A

Found in fatty fish, other plant oils, etc.

Has specific role in brain development

78
Q

Peptide bond

A

Covalent bond between two amino acids

79
Q

What is the peptide bond formed ebtween?

A

C of the carboxyl group and N of the amine group.P

80
Q

Polypeptide

A

Chain of amino acids/polymers.

81
Q

Denature

A

To lose the shape of a protein adn thus, losing function (by exposing to harsh environmental conditions)

82
Q

HOw is a dipeptide made from two amino acids?

A

OH is removed from the carboxyl end of the first amino acid, and H is removed from the amine end of the 2nd amino acid. C from the carboxyl forms a peptide bond with the N of the amino acid. H2O is also produced

83
Q

What does essential amino acid mean?

A

amino acids that one must eat in their exact form, as we don’t have the ability to synthesise them

84
Q

Examples of important proteins in the body

A

Hemoglobin, collagen, keratin, histones, hormones

85
Q

Structure of an amino acid

A

Amine group (NH2)
C
H
COOH (carboxyl group)
R group

86
Q

Why does exposure to help temperatures cause denaturation for proteins?

A

Weaker folds between peptides hold the protein together, so the substrate is able to fit into the receptor.
Exposure to high temperatures break the weak folding bonds, so cannot find into the receptor.

87
Q

R group

A

additional chain of elements coming from the central C in an amino acid. Makes each amino acid unique and gives them chemical properties

88
Q

Hydrophobic interactions

A

When non-polar amino acids move inwards away from polar H2O molcules and thus, towards each other

89
Q

Disulfide bond

A

Covalent bond between the sulfurs of the cysteine’s R group

90
Q

Levels of protein structure

A

Primary
Secondary
Tertiary
Quaternary

91
Q

How does the polarity of an amino acid impact their structure within the protein?

A

Determines tertiary structure of protein. Usually, polar amino acids surrounds the outside of the protein, while hydrophobic ones are in the centre

92
Q

What do the chemical properties fo the R groups determine?>

A

The reactivity of the amino acid

Specific R group -> structure and shape of protein -> function of protein

93
Q

Main categories of R groups

A

Non-polar: 9 (hydrophobic)
Polar: 6 (hydrophilic - form hydrogen bonds)
Charged: 5 (form ionic bonds)

94
Q

Primary structure

A

specific sequence of amino acids joined together by strong covalent peptide bonds

95
Q

What affects primary structure

A

Mutations (i.e. determined by DNA)
Does not denature

96
Q

Secondary structure

A

Hydrogen bonds between C=O carboxyl of one amino acid and the N-H+ of another amino acid. Does not use R groups

Forms either one of two systematic patterns

97
Q

Two systematic patterns of secondary structure

A

Beta-pleated sheet
ALpha helix

98
Q

Alpha helix

A

Polypeptide is wound into a helix. H-bonds are between turns of helix

99
Q

Beta-pleated sheet

A

Sections of the polypeptide run in opposite directiosn, and H bonds form between lines (giving a pleated shape because of bond angle)

100
Q

What affects secondary structure?

A

Not mutation, as R groups are not used

H-bonds will break in extreme enviornments so will lose secondary structure in denaturation

101
Q

Tertiary structure

A

Unique folding that results form specific R group interactions and bonds

102
Q

Types of R group interactions (in order of most to least strength)

A

Disulfide bridges:
Ionic bonds
Hydrogen bonds
Hydrophobic interactions

103
Q

Disulfide bridges

A

strong covalent bonds ebtween sulfur groups of cysteine amino acids

104
Q

ionic bonds

A

hetween two oppositely charged amino aicds

105
Q

hydrogen bond

A

forms between any polar amino acid

106
Q

Hydrophobic interactions

A

tendency of non-polar amino acids to face away from water and towards each oterh

107
Q

Most to least common R group interactions

A

Hydrophobic interactions
hydrogen bonds
ionic bonds
disulfide bridges

108
Q

What affects tertiary structure

A

Extreme environments affect:
- temperature breaks H bonds
- pH change can break ionic bonds

Mutations change amino acids/R groups and alter tertiary structure. Some have more impact
i.e. polar -> polar = minimal
polar -> non-polar = major

109
Q

Quaternary structure

A

Coming together of multiple polypeptides (and some non-popypeptide units) to form the protein

110
Q

How are quaternary strucutre held together?

A

By R group interactions between amino acids of different chains. Same interactions as tertiary but between different polypeptides

111
Q

Does all proteins have a quaternary structure?

A

No, not all

112
Q

NOn-conjugated protein

A

Only contains polypeptide subunits

113
Q

COnjugated protein

A

Contains at least one non-protein component

114
Q

Example of conjugated protein

A

Heme groups

115
Q

Globular proteins

A

Highly folded proteins that end up with a spherical shape.

116
Q

Fibrous proteins

A

Long polypetides that lack tertiary bonds and folding /don’t have a consistent secondary structure.

117
Q

how has cryogenic electron microscopy aided in our understanding of protein structure?

A

Enabled to see very small size. Involves flash freezing proteins in liquid ethane. Images can be obtained using beam of electrons. Software can then develop images and see individual atoms of a profile

118
Q

What is an integral protein?

A

A protein that sits all the way through the whole phospholipid bilayer/membrane. must be amphipathic

119
Q

Examples of important proteins

A

Collagen, insulin, haemoglobin

120
Q

Structure of collagen

A

A fibrous protein (does not fold) made up of three polypeptide chains with repeating amino acid sequences held together by R group bonds.

121
Q

Function of collagen

A

Strong (due to so many bonds) and elastic. used for structural body tissue: ligaments, tendons, cartilage , connective tissue

122
Q

Structure of insulin

A

A non-conjugated globular protein made up of two polypeptide chains folded into a spherical shape and held together by disulphide bridges

123
Q

Function of insulin

A

Hormone that binds to a receptor with a compatible shape. It decreases blood glucose by telling cells to take up carbohydrates

124
Q

Haemoglobin strucyure

A

Globular conjugated protein made up for four polypeptide chains (two alphaglobin and two beta glob in) and four Heme groups

125
Q

Function of haemoglobin

A

O2 attached to each of the Heme groups. Therefore each haemoglobin carries 4 O2, on the surface of red blood cells

126
Q

What part of the protein structure does DNA affect?

A

Primary structure, due to deciding specific amino acid/R groups

127
Q

What determines the tertiary and quaternary structure?

A

Folding by r groups

128
Q

Outline impact of structure change on function

A

DNA -> specific amino acid (primary structure) -> folding by R groups (tertiary and quaternary structure) -> unique shape of protein -> determines what its compatibility -> function.

A change in the shape of the protein (mutation that affects primary structure OR extreme environments which impact tertiary)

IB Biology (10 decks)

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