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Biological Molecules Flashcards

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1
Q

What is a monosaccharide

A

Monosaccharides are individual molecules that make up disaccharides and polysaccharide. Examples include glucose fructose and galactose

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2
Q

What is a condensation reaction?

A

It joins two molecules together with a formation of a chemical bond and involves the elimination of a molecule of water

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3
Q

Hydrolysis reaction

A

Breaks a chemical bond between two molecules and involves the use of a water molecule

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4
Q

What bond forms between two monosaccharides during a condensation reaction?

A

Glycosidic bond

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5
Q

Examples of disaccharides

A

Maltose = glucose + glucose (reducing)
Lactose = glucose + galactose (reducing)
Sucrose = glucose + fructose (non reducing)

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6
Q

What is a reducing sugar?

A

They can donate electrons to other compounds

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7
Q

What are the isomers of glucose?

A

a-glucose and b- glucose

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8
Q

Examples of polysaccharides

A

Starch glycogen and cellulose

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9
Q

Structure properties and function of starch

A

Made of a-glucose,amylose and amylopectin (branched 1-6 glycosidic bonds). Stores excess glucose in plants insoluble and does not effect water potential

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10
Q

Structure, properties and function of glycogen

A

Glycogen long branched bonds 1-6 and is a stores excess glucose as glycogen in animals highly branched for quick hydrolysis of glycosidic bonds for glucose release. Compact good for storage.

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11
Q

Structure, properties and function of cellulose

A

Made of B- glucose long unbranded Chains linked by hydrogen bonds creating microfibrils structural support to cell walls, keeping cell turgid

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12
Q

Function of lipids

A

Source of energy, insulate organisms and waterproofing

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13
Q

Structure of triglycerides

A

Glycerol molecule and three fatty acid chains forming an ester bond by condensation reaction between the 3 OH groups and the glycerol OH group

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14
Q

Properties of triglycerides

A

The fatty acid chains are hydrophobic making them insoluble in water. They can be unsaturated or saturated fatty acid chains.

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15
Q

The function of triglycerides

A

Used as an energy store as there is a lot of energy released when the fatty acid chains are broken

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16
Q

Structure of phospholipids

A

glycerol molecule, phosphate group and two fatty acid chains. There’s an ether bond formed by condensation reaction between the 2 OH groups on the glycerol and the OH group of each fatty acid chain.

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17
Q

Properties of phospholipids

A

The phosphate group is hydrophilic and the fatty acid chains are hydrophobic these conform by layers of membranes

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18
Q

What are saturated fatty acids?

A

They don’t have any double bonds between their carbon atoms as they are “saturated” with hydrogen

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19
Q

What are unsaturated fatty acids?

A

They have double bonds between their carbon atoms which means they contain fewer hydrogen atoms they can bend or kink

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20
Q

Introduction to phospholipid bilayer

A

The phospholipid heads face outwards as they are hydrophilic and their fatty acid tails face inwards as they are hydrophobic . Therefore the centre of the bilayer is therefore hydrophobic so water soluble substances cannot easily pass through

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21
Q

What are proteins?

A

They are polymers made up of monomers known as amino acids

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22
Q

Amino acid structure

A

They have a carboxyl group, amino group, variable group and a hydrogen

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23
Q

What happens when two amino acids joined together?

A

Forms a condensation reaction and a peptide bond releasing a water molecule between the amine group of one amino acid and the hydroxyl group of the other = dipeptide

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24
Q

Describe the primary structure of a protein

A

Determines the number and sequence of amino acids in the polypeptide chain. This can determine the 3-D shape or tertiary structure and can therefore affect the shape of the enzyme active site.

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25
Describe the structure of a secondary protein
Hydrogen bonds formed between amino acids causing it to coil into an alpha helix or fold into a B pleated sheet= stable structure
26
Tertiary protein structure
3D shape of polypeptide chain. Hydrogen bonds, ionic bonds and disulphide bridges form between R groups
27
Quaternary protein structure
Made up of more than one polypeptide chain
28
What is an enzyme
A biological catalyst ( that does not get used up in the reaction ) that speed up the rate of chemical reactions by lowering the activation energy
29
What forms when an enzyme binds to a substrate
An enzyme substrate complex is formed
30
What is the differences between induced fit and lock band key model?
Lock and key: substrate is exactly complimentary to active site Active site does not change shape Induced fit: shape of active site is not exactly complimentary Active site does change shape
31
Name the four main factors affecting enzyme action
Enzyme concentration, substrate concentration, temperature, PH
32
How does increasing enzyme concentration affect enzyme activity
- increases number of active sites - more ES complexes can be formed - rate of reaction will increase until amount of substrate will become a limiting factor
33
How does increasing the substrate affect enzyme activity
- Increase rate of reaction - more collisions so more ES complexes - however when all the active sites are occupied rate of reaction will slow and so increasing the substrate will have no further affect
34
How does increasing the temperature affect the rate of enzyme activity
- increases rate of reaction as there is more kinetic energy so molecules move faster increasing the amount of collisions for more ES complexes - each enzyme has an optimum temperature increasing the temperature decreases rate of reaction - too high temperatures denatures the enzyme as the protein tertiary structures bonds are broken and so the active site changes shape and can no longer form es complexes
35
How does increasing the PH increasing the rate of reaction
- all enzymes have an optimum PH so above and below optimum PH disrupt the ionic and hydrogen bonds holding the tertiary structure - extremes PH can change the active site and no more ES complexes can be formed as substrate no longer fits enzyme is therefore denatured
36
Name the two types of enzyme inhibition
Competitive and non competitive
37
Describe the competitive inhibition
Similar shape to substrate Compete with substrate to bind to active site Block the active site so the substrate cannot bind so no more ES complex
38
Describe non competitive inhibition
Do not bind to active site as have different shape to substrate Bind to allosteric site Causes the enzymes active site to change shape no longer complimentary to substrate so no more ES complexes
39
How does increasing the substrate concentration affect the competitive inhibitor
Increases rate of reaction as it will reverse the effects of competitive inhibitor as the substrate will outcompete the inhibitor for active site
40
How does increasing the substrate concentration affect the non competitive inhibitor
Will not affect rate of reaction as the substrate cannot bind to active site
41
What are nucleic acids
Biological macromolecules, made up of nucleotides
42
What is each nucleotide made of
A phosphate, ribose sugar and a base
43
What are the two types of nucleic acids?
Ribonucleic acid (RNA) , Deoxyribonucleic acid (DNA)
44
45
Where does the condensation reaction join together on the nucleotides
Between the phosphate group of one and a carbon of the penthouse sugar on the other = phosphodiester bond
46
What are the four bases of DNA
Thymine, Adenine, guanine, cytosine
47
How do the bases pair up
Via complimentary base pairs, thymine pairs with adenine and guanine pairs with cytosine
48
Adenine is a purine what pyrimidine does it pair up with?
With thymine in DNA and Uracil in RNA forming two hydrogen bonds
49
Cytosine is a pyrimidine what purine does it pair up with?
Guanine forming three hydrogen bonds
50
What is the structure of ATP
Adenosine triphosphate- ribose sugar, adenine base, 3 phosphate groups
51
Hydrolysis of ATP
ADP > PI catalysed by the enzyme ATP hydrolase
52
What is the word for condensation reaction of ATP
Phosphorylation
53
Why is water a polar molecule
O is more electronegative than H so attracts the electron density in the covalent bond more strongly
54
State 4 properties of water
- metabolite/ solvent for chemical reactions - high SHC - high latent heat for vaporisation - cohesion between molecules
55
Why is water significant for living organisms
- solvent for polar molecules during metabolic reactions - enables organisms to avoid fluctuations in core temperature - cohesion- tension of water molecules in transpiration stream
56
What are inorganic ions and where are they found in the body?
-ions that do not contain carbon atoms -found in cytoplasm and extra cellular fluid - may be high or low concentrations
57
Explain the role of hydrogen ion in the body
High conc of H+ = low pH H+ ions interact with H-bonds & ionic bonds in tertiary structure of proteins which can cause them to denature
58
Explain the role of iron into in the body
Fe2+ bonds to porphyrin ring to form haem group in haemoglobin Haem group has binding site to transport 1 molecule of O2 around body in bloodstream 4 haem groups per haemoglobin molecules
59
Explain the role of sodium ions in the body
Involved in co transport for absorption of glucose and amino acids in lumen of gut Involved in propagation of action potentials in neurons
60
Explain the role of phosphate ions in the body
Component f -DNA -ATP NADP - cAMP

Biology (3 decks)

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