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Biological Molecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Carbohydrates

A

Made of carbon hydrogen oxygen

Mostly made by plants

Important energy resource

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2
Q

Positive Benedict’s

A

Blue to red

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3
Q

Starch -iodine

A

Brown to blue black

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4
Q

General carb formula

A

(Ch2o)n

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5
Q

Fructose symbols

A

C6h12o6

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6
Q

Monosaccharides

A

Consist of one sugar unit where number of carbon atoms can very

Glucose fructose ribose

(Ch20)n

Soluble in water

Often taste sweet

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7
Q

Ribose formula

A

C5h10o6

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8
Q

Cellulose

A

Beta

1,4 glycosidic bonds

Plants

Structural ridigty ,prevents burst and maintains turgid

Unbeanched chains linked together

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9
Q

Disaccharide

A

Consist of 2 monosaccharides connected by a glycosidic bond formed by a condensation reaction where a water molecule was lost

Lactose sucrose maltose

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10
Q

Monomer +monomer

A

Disaccharide

Water molecule removed by condensation reaction

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11
Q

Maltose

A

Glucose + glucose

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12
Q

Starch

A

Alpha

1,6

1,4 glycosidic bond

Formed by condensation reactions

Branched and h branched chains

Found in plants seeds and storage organs

Energy storage

Large and insoluble

Iodine

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13
Q

Sucrose

A

Glucose +fructose

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14
Q

Polymer

A

Large complex molecules composed of long chains of monomers joined together

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15
Q

Unbranded chains

A

Linked together by ma h h binds adding to strength microfibriks join together to form fibres adding more strength

Microfiibrriks join together to form fibres adding more strength

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16
Q

Adaptions of being large and insoluble

A

No diffusion out of cells

Compact a lot can be stored in snakkk space

Branched many ends for enzymes to start hydrolysis

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17
Q

Polysaccharide

A

Chains of ma h sugar units can be straight or branched

Glycogen cellulose starch

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18
Q

Example of monomers

A

Glucose

Amino acids

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19
Q

Lactose

A

Glucose + galactose

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20
Q

Monomer

A

Small basic molecule units

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21
Q

Glycogen

A

Alpha

Glycosidic bonds formed by condensation reactions

Branched

Animals fungi bacteria

Storage polymer and hydrolysed to release glusocse for resp

Large and insoluble

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22
Q

Why does sucrose need to be broken down.

A

To become a reducing sugar

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23
Q

What carb has 1!6 glycosidic bind

A

Amylopectin

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24
Q

Why add ethanol to lipids

A

To dissolve it

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25
Q

Polar (charged substances )

A

Soluble in water

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26
Q

Lipids

A

Contain carbin hydrogen and oxygen

Insoluble in water

Soluble in all and acetone (organic solvents )

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27
Q

Role of lipids

A

High in energy

When oxided t provide twice the energy and also release water

Excessive dietary fat intake which is associated with obesity ,diabetes,cancer

Saturated fat found in dietary products and animal fats lead to fatty plaques in arteries

In cell membrane

Phospholipids contribute to flexibility of membranes

Solubilise fat for so,unless vitamins

Protection in kidneys

Insulation for respiration and maintain 37 for chem reaction

Waterproof

Insoluble I. Water does not dissolve in cytoplasm

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28
Q

Triglycerides

A

Most common lipids in food

Compromised of 1 glycerol man’s 3 fatty acid molecule joined by ester bond via condensation reaction

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29
Q

Fatty acids

A

Long hydrocarbo. Chain which a carboxy group

No c-c double bonds

Mini unsaturated or poly unsaturated

Nature depends on which fatty acids are present

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30
Q

Structure of triglycerides

A

High ratio of energy storing carbon-hydrogen bonds to carbin atoms

Good storage molecule

Release water darn oxidised due to high ratio of hydrogen and oxygen and therefore provide an important source of water fir organisms in dry desserts

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31
Q

Phospholipid

A

One of fatty acids molecules is replaced with a phosphate molecule

Made of hydrophilic head and hydrophobic tail

Polar molecule as two ends behave different

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32
Q

Importance of hydrogen bonds

A

1)cross links between chains

2)forms microfibrillis

3)hydrogen bonds strong in large numbers

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33
Q

Polymer

A

Large molecules consisting of large numbers of repeating units connected by covalent bonds

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34
Q

Monomer

A

Small my,wake that maybe come chemically bonded to other monomers to form a polymer

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35
Q

Amino acid =

A

Minomer

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36
Q

Polypeptide

A

Polymer

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37
Q

Types of r groups

A

Hydrophilic

Hydrophobic

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38
Q

Hydrophilic

A

Polar -acid or basic

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39
Q

Hydrophobic

A

Non polar

Acid and basic r group will attract each other

Hydrophobic group and will attract each other

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40
Q

What type of bind does carb have

A

Glycosidic

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41
Q

What type of bind does a lipid have

A

Ester

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42
Q

What type of bind does protein have

A

Peptied

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43
Q

Why are hydrogen binds important in cellulose molecules

A

Give add strength and make mucrofibrrikis which join together to form fibres
Cross links in chains of hydrogens
Strong in large numbers

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44
Q

Why spiral shape in hydrogen is important

A

Compact occupies small space and highly packed

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45
Q

What is a. Unsaturated fatty acid

A

It has one or more double carbin carbin bind
2 carbind with one hyrigrgen

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46
Q

How many molecules in triglycerides

A

4

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47
Q

Large and insoluble

A

Compact
Occupy small space
Branched ends
No diffusion out of cells

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48
Q

What bind is formed in a condensation reaction

A

Glycosidic bond

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49
Q

Hydrolysis

A

When water is added to a disaccharide under suitable conditions it breaks the glycosidic bond releasing the monosaccharides

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50
Q

Cellulose is a

A

Polysaccharide

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51
Q

Polysaccharide

A

Polymers formed by combining together many monosaccharides molecules which are joined by glycosidic bonds that were formed by condensation reactions .

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52
Q

How is Starch suited

A

Insoluble - doesn’t affect water potential so water is not drawn in to cells by osmosis
Large and insoluble - it doesn’t diffuse out of cells
Compact-so a lot of it can be stored un a small space

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53
Q

Glycogen adaptions

A

Insoluble -does not rent to draw water into the cells by osmosis
Does not diffuse out of cells
Compact sores in small space

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54
Q

How is cellulose adapted

A

Straight unbranched chains
Beta glusocse
Hydrogen bonds form cross links between adjacent chains strength
Molecules grouped to form microfibriklis

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55
Q

Role of lipids

A

1)source of energy
2)waterproofing
3)insulation
4)protection

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56
Q

Source of energy

A

When oxidised lipids provide 2x the energy as the same mass of carbohydrates and release valuable water

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57
Q

Waterproofing

A

Lipids are insoluble in water therefore useful as waterproofing
Both plants and waxy lipid cuticles that conserve water

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58
Q

Protection

A

Fat us often stored around delicate organs such as kidneys

59
Q

Triglycerides

A

Three fatty acids combined with glycerol
Each fatty acid forms an ester bind with glycerol in condensation reactions

60
Q

Saturated fatty acids

A

All carbon atoms are linked to the maximum possible number of hydrogen atoms

61
Q

Phospholipids

A

Hydrophobic tail - orients itself away from water but mixes rweadily with fat
Hydrophilic head interacts with water but not with fat

62
Q

Polar meaning

A

Molecules that have two ends that behave differently

63
Q

primary structure

A

the sequence of amino acids in the polypeptide chain
detrmines shape and function
peptide bond

64
Q

what makes dipeptide bonds

A

condesnation reaction

65
Q

2 amino acids

A

dipeptide more than two amino acids =polypeptied formed by condesnationreactions

66
Q

what determines sequence of amino acids

A

DNA base sequence of the gene that codes for the polypeptide in nucleus by transcription.

67
Q

secondary structure

A

strings of amino acids twist to form either an alpha helix of a beta plated sheet
peptide and hydrogen bonds formed

68
Q

alpha helix

A
69
Q

tertiary structure

A

fold to form a 3d shape
chemical bonds and hydrophobic interactions between r groups maintains shape
some r groups are polar meaning they are hydrophillic and attract to other polar r groups

non-polar r groups are hydrophobic and face inside the protein

ionic bonds if r groups are charges and disulphate bonds

70
Q

in a tertiar structure what shape does polypeptide form

A

a 3d structure

71
Q

types of bond in tertiary structure of protein

A

1)disulphide bridges -strong covalent bonds and not easily broken
2)ionic bonds
3)hydrogen bonds

72
Q

disulphide bridges -

A

strong covalent bonds and not easily broken

73
Q

ionic bonds

A

ionic bonds weaker than disulphide bonds and easily broken by change in PH

74
Q

hydrogen bonds

A

hydrogen bonds -numerous but easiy broken especially by high temperatures

75
Q

quzternary strucutre

A

determines by several polypeptide chains combining to form a big protein

76
Q

conjugated protrin

A

a non protein molecule added
eg-haemoglobin contains an iron group

77
Q

explain how the primary structure of an enzyme determines its three dimensional shape and properties

A

1)primary structure isnthe sequwnce of amino acids in a polypeptide chain
2)determining positiin of the bonds and active site hape
3)complimentary

78
Q

globular proteins

A

fold into compact spherical shape
usually soluble
carry out metabolic functions
-quaternary

79
Q

examples of globular protiens

A

enzymes
haemoglobin
antibodies

80
Q

fibrous proteins

A

form long parallel chains crosslinked for stabiliity
they are usually inoluble and have structural functions

81
Q

examples of fibrous proteins

A

keratin
collagen
biotin

82
Q

collagen

A

-primary strcutre is unbranched polypeptide chains

-secondary structure polypeptied chain very tightly wound

-lots of glycine-helps close packing

-found in tendonds
-not souble
polymer of amino acid

83
Q

Amino acid groups

A

1)amino group
2)carboxyl group
3)hydrogen group
4)hydrogen atom
5)r group

84
Q

Amino acid definition

A

Basic monomer units which combine to make up a polymer called a polypeptide

85
Q

Formation of peptide bond

A

Amino acid monomers combine
Removal of water molecule in condensation reaction
Broken by hydrolysis to give two Camino acids

86
Q

Primary structure of proteins

A

Series of condensations many amino monomers join in polymerisation
Creating polypeptide sequence of amino acids in a polypeptide chains forms the primary structure of any protein
Determined by dna
Determines shape and function

87
Q

What can a change in amino acid sequence do

A

Change in shape of a protein and may stop carrying out its function
Protein show especifc to its function

88
Q

Secondary structure
Of proteins

A

NH pos and -c=o groups neg
Readily form weak bonds -h2 bonds
Long peptide chain twisted into 3d shape
Alpha helix

89
Q

More on ionic bonds

A

Formed between any carboxyl and amino groups that are not involved in forming peptide bonds
Weaker than disulphide binds
Easily broken due to change in ph

90
Q

Ina tertiary structure what makes protein distinctive

A

3d shape
How functions
Be recognised by other molecules
Interact with molecules in a specific. Way

91
Q

Quaternary structure

A

Individual polypeptide chains linked in various ways
Non protein-prosthetic groups

92
Q

why is solid water less dense than liquid water

A

because of hydrogen bonds

93
Q

why is water dipolar

A

pair of shared electrons in the oh bonds are more attracted to the oxygen atom
therefore uneven dsutrubution of charge
oxygen-neg
hydrogen-pos
therefore dipolar

94
Q

why is water polar

A

electrons are attracted more strongly to the oxygen than the two hydrogens

95
Q

why polar is useful

A

excellent solvent
useful for transport of substance
reactions happen much faster in aqueous solution

96
Q

water properties

A

-a high specific heat capacity
because of hydrogen bonds
-takes a lot of energy to change the temp which reduces the dramatic changes that would affect enzymes
-aquatic animals
-high latent heat of vaporisation
-because of hydrogen bonds
-lots of energy required to evaporate the water so it has a cooling effect like sweating for animal cells and transpiration of plants
-cohesion between molecule
-hydrogen bonds
-creates surface tension providing a habitat
for small insects
-key to transports n the xylem
-adhesion because of hy2 bonds
-involved in transport in the xylem
-water has a solid for that floats because of hydrogen bonds where ice is less dense than water and this produces ice caps with produce a habitat eg.polar bears

97
Q

importance of water to living orgsnisms

A

1)to breakdown complex molecules by hydrolysis
2)chemical reactions take place in the aqueous medium
3)reactant for photosynthesis

98
Q

water being a solvent

A

1)gases scubas oxygen and carbon dioxide
2)wastes such as urea and ammonia
3)inorganic ions and small hydrophilic molecules such as amino acids ,monosaccharides and atp

99
Q

incompressibility of water

A

-much less distance between the molecules in liquid than in a gas
-provide support for the hydrolystatic skeleton of animals such as earthworms and give turgor pressure in plants

100
Q

maximum density of water at 4 degrees

A

-most liquids contract on cooling reaching maximum density at their freezing point
-water reaches max density at 4 degrees
-ice formed is less dense than the cold water so it floats on top and insulates the water below it. lakes rarely freeze solid and the aqautic life can survive freezing temps.

101
Q

Isomers

A

Organic molecules that have the same chemical formula but different structural formula; [1 mark]

102
Q

how cellulose gives cotton strength

A

The many hydrogen bonds found between the parallel chains of microfibrils; [1 mark]
Cellulose fibres and other molecules (eg. lignin) found in the cell wall form a matrix; [1 mark]

103
Q

When Benedict’s reagent is mixed with sucrose solution there is…

A

No colour change BECAUSE sucrose is a non-reducing / not a reducing sugar

104
Q

two similarities between glycogen and starch

A

Both are made of the same monomer, alpha/∝ glucose
Both are branched molecules
Both contain 1,4 glycosidic bonds and 1,6 glycosidic bonds

105
Q

two differences between glycogen and starch

A

Starch is made up of amylose and amylopectin polysaccharides
Glycogen is more highly branched than starch (amylopectin)
Glycogen has more terminal ends than starch

106
Q

The reaction that converts glucose into starch

A

Is a condensation reaction
That forms glycosidic bonds (between monomers
Chains are formed with 1-4 links/bonds
Branches are formed with 1-6 links/bonds
Water is produced (as a by-product)

107
Q

explain one reason why peas use starch for storage rather than glucose

A

Starch is insoluble SO does not affect water potential / has no osmotic effect / cannot leave the cell
Starch has a coiled/helical/spiral structure SO can fit many molecules into a small area / compact / tightly packed

108
Q

chemical formula of maltose

A

C12H22O11

109
Q

saturated fatty acids have the least amount of oxygen

A
110
Q

what bonds to primary structure have

A

polypeptide bonds

111
Q

secondary structure bonds

A

hydrogen bonds

112
Q

tertiary bonds

A

disulphide
ionic

113
Q

conditions for a reaction to occurf

A

1)reactants must collide with suffient energy to alter the arrange meant of the atoms
2) The free energy of the products must be less than of the substrate
3)many reactions require an initial amount of energy to start. the minimum about of energy needed is the activation energy.

reactants energy must be more than the products

114
Q

anabolic

A

requires energy

115
Q

catabolic

A

releases energy

116
Q

activation energy

A

-the energy of products must be lower than that of the substrates
-subsgtarte molecules must collide with sufficient energy to start the reaction
-enzymes lower the activation energy by stretching or pushing molecules

117
Q

explain how the 3d structure of proteins enable enzymes to preform their function as biological catalyst

A

1)tertiary structure-of the protein provides an active site on the surface of the molecule
2)the complimentary substrate molecule fits into the active site forming enzyme substrate complex
3)products form released from the active site having the enzyme unchanged and ready to combine with more substrate molecules .

118
Q

the induced fit model

A

-two advantages compared to lock and key
-it explains how enzymes may exhibit broad specifity eg.bonding to variety of lipids
-it explains how catalysts may occur where conformational change stresses bonds in the substrate increasing reactivity

119
Q

describe the induced fit model of enzymes action and how an enzyme acts a catalyst

A

induced model shows broad specificity and the active site is relaxed which allows it to modify so its complimentary to the substrate as bonds break down to distort the shape of the active site an forms enzyme substrate complexes reducing activation energy

1)substrate binds to the active site
2)active site changes shape

120
Q

Enzymes

A

Globular proteins that act as a biological, catalytic
Speed up reaction

121
Q

anabolic reactions

A

building for complex molecules from simpler ones by drawing two or more substrates into the active site forming bonds between them and realising a single product
eg.protein synthesis and photosynthesis

122
Q

catabolic reaction

A

involve the break down of complex molecules into simpler products which happens when a single substrate is drawn into the active site and broken apart into two or more distinct molecules

123
Q

metabolism

A

sum of all the chemical reactions
eg.hydrolysis

124
Q

catalyst

A

a substance that speeds up reactions without changing the products

125
Q

metabolic pathway

A

sequence of enzymes controlled reactions

126
Q

specificity

A

only able to catalyst specific reactions

127
Q

substrate

A

the molecules the enzymes works on

128
Q

product

A

molecules produced by enzymes

129
Q

enzymes bringing substrate molecules together

A

anabolic reactions

130
Q

enzymes being a globular structure

A

active site has a specific shape due to tertiary structure of protein

a change in shape of the protein affects shape of active site and the function of the enzyme

131
Q

how would you measure the effect of an enzyme

A

-compare uncatalysed rate with catalysed
-enzymes can increase rate by a factor of between 10^8 to 10^26

132
Q

enzyme binds to the substrate to form an enzyme substrate complex

A
133
Q

factors affecting enzymes

A

-temperature,
pH,
enzyme concentration, substrate concentration,

134
Q

what is rate of enzyme action dependent on

A

number os substrate molecules present

135
Q

rate of reaction levels off

A

max rate of reaction (max) reaches saturation point as all active sites are occupied

136
Q

some active sites free at lower substrate concentrations

A
137
Q

why enzyme conc levels off

A

max rate of reaction (max) reaches saturation point as all substrate are occupied

138
Q

thermophilic bacteria

A

have enzymes with optimum temp of 85 degrees

139
Q

pepsin ph

A

2

140
Q

tripsin ph

A

7/8

141
Q

why ph affects proteins

A

ph affects fermentation of h bonds and sulphur bridges in protein and so affects shape
change in ph also alters the charges on the amino acid that make up the active site substrate complex cannot form.

142
Q

name the part of the pancreatic cell that forms the inactive form of trypsin

A

ribosomes

143
Q

suggest the advantage of producing trypsin in an active form of molecules

A

it doesn’t digest/break down protein in the cells - good that trypsin inactive in the pancreas so tissue is not destroyed

144
Q
A

Biology (58 decks)

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