Biological Molecules Flashcards

1
Q

Bond formed and polymer for
Amino acids
Nucleotide
Monosaccharides

A

Amino acids - peptide bond, form proteins (polypeptides)
Nucleotide - phosphodiester bond, forms nucleic acids (RNA, DNA)
Monosaccharides - glycosidic, polysaccharides

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2
Q

Constituent elements of
Carbohydrates
Proteins
Lipids
Nucleic acids

A

Carbs - CHO (more O, less H)
Proteins - CHONS
lipids - CHO (more H, less O)
Nucleic - CHONP

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3
Q

Water is a […] molecule

A

Polar

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4
Q

Formation of H bonds in water

A
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5
Q

Properties and roles of water

A

+ solid ice = less dense than water (l) therefore surface of ice = habitat for organisms
Water beneath ice remains insulated and aquatic organisms don’t freeze to death

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6
Q

Alpha vs beta glucose

A
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7
Q

3 diff disaccharide we have to know

A

Maltose
Sucrose
Lactose

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8
Q

Constituents of the 3 disaccharides

A

a gluc + a gluc -> maltose & water (1,4 bonds)

a gluc + fruc-> sucrose & water (1,2 bond)

a gluc + b galactose -> lactose & water (1,4 bond)
Glycosidic bonds also form where the 2OH groups of separate monosaccharide are adjacent

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9
Q

Carbohydrate function

A

Energy store, energy source, structural units

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10
Q

Deoxyribose vs ribose

A
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11
Q

Deoxyribose vs ribose

A
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12
Q

Reducing vs non-reducing sugars

A
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13
Q

Starch features & function

A
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14
Q

Amylose vs amylopectin

A
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15
Q

Function of cellulose

A

Main structural constituent of plant cell walls

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16
Q

Features of cellulose

A
  • high tensile strength
  • insoluble in water
  • flexible
  • strong microfibrils
  • fibrous
  • not granular
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17
Q

Cellulose structure details

A

-b glucose monomers 1,4 glycoside bonds

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18
Q

Why are branched polysaccharides better for energy storage

A
  • lots of branches for enzymes to attach to
  • compact molecules
  • high energy content for their mass
  • can quickly be hydrolysed
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19
Q

What is glycogen

A

Main energy storage polysaccharide found in animals and fungi

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20
Q

Why is glycogen better than amylopectin etc

A

Forms more branches than it so more compact
In animals as it’s Better for storage = more useful for MOBILE animals

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21
Q

Glycogen structure

A
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22
Q

Lipid characteristics

A
  • macromolecules
  • non polar
  • have a chain of carbon atoms as a backbone
  • insoluble in water
  • soluble in alcohol
23
Q

Saturated vs unsaturated lipids

A

Unsaturated = double bonds in C=C

24
Q

Effect of double bond in unsaturated lipids

A

Causes molecule to bend / kink
So less able to pack tighter nicely, therefore dense
So b.p. Less

25
How are triglycerides formed from 1 glycerol & 3 fatty acids
26
Glycerol + fatty acid structure
27
Functions of triglycerides
28
What are phospholipids
Modified triglycerides One fatty acid change replaced by inorganic phosphate ion (PO4)3-
29
Phospholipids made up of? And function
Form selective permeable phospholipid bilayer Made up of 1 glycerol, 2 fatty acids & a phosphate group therefore polar
30
Phospholipids in water? E.g. how does hydrophobia & philia play a role
31
What roles of the phospholipid bilayer are there?
Forms the cell membrane, (which plays a role in Compartmentalisation: to separate the sites of chemical reactions and allow for the formation of concentration gradients) Separate as the cytoplasm from outer (aq) environments
32
What are sterols and their function
33
Roles of lipids
Membrane formation (hydrophobic barrier) Hormone production Electrical insulation (neuron myelin sheath). Waterproofing (birth feathers, plant leaves)
34
Lipid identification emulsion test steps
1. Mix sample with ethanol (if solid should be ground up first) 2. Mix solution with water & shake 3. If the white emulsion forms @ top, indicator of lipid
35
General structure of an Amino acid
36
How peptide bond form
37
Oligopeptide vs polypeptide
Oligo = short chain of amino acids linked together Poly = long chain
38
How many protein structures
4
39
Protein primary structure
The sequence of amino acids in a polypeptide chain, specific to each protein
40
Protein secondary structure
Formed due to hydrogen bonds forming between amine group and carboxylic group which leads to the folding into a beta pleated sheet or coiling into an alpha helix H bond can be broken at high temps & pH changes
41
Tertiary structure + types of bonds formed in it
The further coiling and folding of the amino acid to form the overall 3D shape of a protein & additional bonds being formed between R groups Hydrogen - between R groups = weakest bind Ionic - between pos & neg R groups Disulfide (strong cov bonds between 2 cysteine R groups (these contain S atoms & can be broken by oxidation) Weak hydrophobic interactions - between non-polar, hydrophobic R groups, to cause twisting of amino acid chains
42
Quaternary structure of proteins
Consisting of many polypeptide chains Contains b and alpha subunits & peptide bonds The arrangement of 2nor more polypeptide chains in a protein make up its quaternary number
43
Types of proteins
Globular & fibrous
44
Globular protein features / structure / function
45
Examples of globular proteins and what they do
46
What are conjugated proteins + example
Haemoglobin
47
Haemoglobic structure & function
48
Fibrous protein features
49
3 examples of fibrous proteins?
Keratin Elastins Collagen
50
Keratin function
Provides mechanical protection & is waterproof Impermeable barrier to infection Found in nails and hair
51
Elastins function
Allows stretch and recoil in lungs + in blood vessels to maintain blood pressure
52
Collagen function and structure
Provides mechanical strength: Withstands arteries high pressure Tendons & binds made of collagen Connective tissue Structure Every 3rd amino acid = glycine = allows polypeptide chain closeness Formed of 3 polypeptide chains with H bonds between them, forming a triple helix Adjacent molecules joined by cross links which are staggered in the ends of fibrils
53
Give 3 functions of the cytoskeleton
Hold organelles in place Provide strength & support (not structural) Movement of chromosomes