B3 - Biological molecules Flashcards

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1
Q

Why is water a polar molecule?

A
  • Oxygen is more electronegative, so has stronger attraction to the electrons in the covalent bond.
  • Oxygen is partially negative, Hydrogen is partially positive (due to its weaker electronegativity compared to the oxygen)
  • Uneven share of electrons created a dipole (positive and negative region)
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2
Q

Water has strong hydrogen bonding between hydrogens and oxygens of adjacent molecules, which gives water its properties. What are these properties of water? (6)

A

High specific heat capacity:
- Lots of thermal energy required to raise temp of 1kg of a substance by 1d.c
- Large energy to break H-bonds.
-Temperature doesn’t fluctuate drastically
- Provides suitable habitats
- Maintains temp in body and cells.

High specific latent heat of vaporisation:
- Large energy required to change state liquid to gas(due to many H-bonds).
- acts as a coolant for organisms as only a little water needs to evaporate for organism to lose a lot of heat.

Solvent:
- water = polar, so can dissolve ions
- Act as medium for chemical reactions
- Help transport dissolved compounds in & out cell.

High boiling point:
-large energy to break H-bonds & inc H2O temp

Ice:
- Ice less dense than liquid state, as H-bonds produce a solid lattice structure with polar molecules more spread out in a fixed position.
- Same volume but more area covered.
- Ice floats above water and can insulate aquatic organisms living underneath.

Cohesion & adhesion:
- H-Bonds allow strong cohesion between water molecules (stick together)
- creates surface tension where water body meets air, forming a film for insects to walk on
- adhesion to other molecules e.g. cellulose to move up xylem.

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3
Q

Name 3 monosaccharides (one simple sugar)

A
  • glucose
  • galactose
  • ribose
  • fructose
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4
Q

Lactose and sucrose are both disaccharides (double sugars). What monosaccharides are they made from?

A

Lactose:
glucose + galactose

Sucrose:
glucose + fructose

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5
Q

What is the difference between alpha and beta glucose?

A

Alpha:
OH group is on the bottom of carbon 1/ below the ring
Beta:
OH group is o the top of carbon 1/ above the ring.

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6
Q

Glucose is highly soluble and can be dissolved in the cytosol of the cell. How is glucose so soluble?

A
  • Due to it’s polarity It can H-bond to water
  • H-Bond forms between hydroxyl group and water
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7
Q

What is the bonding called between monosaccharides?

A

glycosidic bonding

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8
Q

What is a condensation reaction in carbohydrates?

A

when the hydroxyl groups of two monosaccharides join to form a disaccharide.

‘condensation’ because water is also released.

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9
Q

What are the 2 polysaccharides in starch? Explain their bonding.

A

Amylose:
- alpha glucose joined by 1-4 glycosidic bonds
- bonding angle causes chain to twist & form helix shape, which is stabilised by H-bonding.
- more compact, less soluble.

Amylopectin:
- has 1-4 AND 1-6 glycosidic bonds
- gives it a branching shape

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10
Q

What are the differences between starch and glycogen?

A

glycogen:
- Stores as small granules.
- Animals store carbohydrates as glycogen (eat starch but store as glycogen)
- less dense, more soluble than starch so can be broken down more rapidly due to higher metabolic requirements in animals.

Starch:
- Plants store glucose as starch
- stored as starch grains in plastids
- plastids have green chloroplasts and colourless amyloplasts

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11
Q

What is a hydrolysis reaction?

A
  • Reverse of condensation
  • Addition of water to break bonds
    e.g. starch & glycogen undergo hydrolysis reactions to release glucose.
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12
Q

Describe the properties of cellulose.

A
  • fibrous
  • very strong & prevents cell bursting
  • structural role
  • beta 1-4 glycosidic bonds (has to flip to react)
  • Hard to break down due to straight chain molecule
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13
Q

What test is used for carbohydrates?

A

Benedict’s - Copper (II) sulfate (alkaline solution)

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14
Q

Describe the set up for benedict’s test of a reducing sugar. (3)

A
  • monosaccharides = reducing sugars (donate electrons to reduce another molecule)
    1) Place sample in boiling tube. If not liquid form, grind or blend in water
    2) Add equal volume of benedict’s solution
    3) Heat mixture gently in boiling water ~5 mins.
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15
Q

Describe and explain the colour changes in a Benedict’s test for a reducing sugar.

A

Reducing sugars add electrons to blue Cu2+ ions, making a brick-red precipitate, indicating a positive result.

Traffic light colour change
green: low conc
yellow: medium conc
red: high conc

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16
Q

Describe the benedict’s test for a non-reducing sugar.

A
  • nonreducing won’t react with solution
  • stays blue = negative result
  • if sucrose (non-reducing) boiled with HCl to hydrolyse into glucose + fructose, then warmed with benedict’s, then the test will be positive.
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17
Q

What is the test for starch?

A
  • Iodine test
  • Iodine drops dissolved in potassium iodide solution and mixed with sample.
  • If turns purple/black starch is present = positive result.
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18
Q

Lipids are stored in adipose tissue. What are the three main roles of adipose tissue? (3)

A

Heat insulation:
- under skin, reduces heat loss in mammals

Protection:
- Around delicate organs, cushioning them against impacts

Hormonal communication:
- lipids are the basis or many hormonal molecules.

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19
Q

What are the two types of lipids? Explain them in detail.

A

Triglycerides:
- Main components of fats & oils
- non polar & hydrophobic
- consists of glycerol (alcohol) and fatty acids (carboxylic acids, which can be saturated, mono-unsaturated, or poly-unsaturated)

Phospholipids:
- modified triglycerides (contain phosphorus)
- 2 fatty acids and 1 phosphate ion bonded to 1 glycerol
- Amphipathic (hydrophilic/polar phosphate & hydrophobic/non-polar fatty acids)

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20
Q

Phospholipids can form bilayers and monolayers. How are they formed?

A

hydrophobic tails point to centre of sheet, protected from water by hydrophilic heads.

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21
Q

Phospholipids can form bilayers and monolayers. How are they formed?

A

hydrophobic tails point to centre of sheet, protected from water by hydrophilic heads.

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22
Q

Triglycerides are formed by esterification. How is an ester bond formed?

A

hydroxyl (OH) group of glycerol bonds with the carboxyl group (COOH) of fatty acids.

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23
Q

What is a sterol? Give an example.

A
  • steroid alcohols
  • Have hydrophobic & hydrophilic properties

cholesterol:
- made in liver & intestines
- Regulate stability & fluidity of cell membranes (maintain at low temp so not too fluid)

24
Q

What is the emulsion test?

A
  • test for lipids
  • mix sample with ethanol, then mix solution in water and shake.
  • white cloudy emulsion layer forms on top if lipid present.
25
Q

Name 3 biological molecules formed by proteins

A
  • enzymes
  • cell membrane proteins
  • hormones
  • transplant & structural proteins
  • contractile proteins
26
Q

What roles do proteins have? (2)

A
  • structural (body tissue)
  • catalytic (enzymes)
  • signalling (hormones & receptors)
  • immunological (antibodies)
27
Q

How many amino acids are in a protein?

A

20

28
Q

What 3 groups do amino acids have?

A
  • amine group
  • carboxyl group
  • R group
29
Q

How is a peptide bond formed between amino acids?

A
  • Hydroxyl in carboxyl group reacts with hydrogen in the amine group of another amino acid.
  • Remaining carbon atom bonds to nitrogen of the other amino acid
  • forms a peptide bond (covalent)
30
Q

Describe the primary structure of a protein. (2)

A
  • the sequence of amino acids joined by peptide bonds
  • determined by info carried in DNA ( instructs cell to add certain amino acids in order)
  • Affects shape and function of protein
31
Q

Describe the secondary structure of a protein.

A

H-bonds form between hydrogens and oxygens of different peptide bonds

alpha helix shape: H-bonds every 4th peptide
beta pleated sheet: parallel peptide bonds

32
Q

Describe the tertiary structure of a protein and the types of bonding. (5)

A
  • folding into final shape
  • Interactions between R-groups

Types:
- Hydrogen - weakest but most common
- Ionic - between + & - Rgroups
- Hydrophobic/philic - nonpolar/polar interactions
- Disulfide - strong covalent bonding cysteine Rgroups (contain sulfer)

33
Q

Describe the quaternary structure in a protein.

A
  • more than 1 polypeptide chain (subunit)
  • e.g. haemoglobin has 2 alpha and 2 beta subunits.
34
Q

What do the enzymes catalase and amylase do?

A

catalase:
- converts hydrogen peroxide(harmful) to water & oxygen (prevents damage)

amylase:
- hydrolyses starch into simple sugars in mouth & small intestines
- secreted by salivary glands & pancreas.

35
Q

What are globular proteins? (3)

A
  • compact
  • SOLUBLE
  • folded into 3D spherical molecules (hydrophilic R-group on outside, hydrophobic on inside)
  • Have a metabolic role
36
Q

Give an example of a globular protein in detail.

A

Insulin:
- hormone that regulates blood glucose concentration
- Fit into specific receptor on cell-surface membrane. (precise shape)
- 2 polypeptide chains held by 3 disulfide bridges.

37
Q

What is a conjugated protein? Give an example.(3)

A
  • Globular protein with a prosthetic group

Haemoglobin
- quaternary (2 beta & 2 alpha subunits)
- Each polypeptide is different (4 genes needed)
- subunits have haem group with Fe2+
- Fe2+ responsible for red pigment in blood
(Binds w/ O2 & transports around body).

38
Q

What is a fibrous protein? (3)

A
  • strong
  • INSOLUBLE
  • long polypeptide chains with cross-linkages due to H-bonds
  • repetitive & limited amino acid sequence = organised structure.
39
Q

Give an example of a fibrous protein in full detail. (there are 3 you should know of).

A

Collagen:
- tensile strength
- connective tissue in skin & ligaments
- 3 polypeptides coiled into twisted rope, forms a twisted strand structure.
- Every 3rd amino acid is glycine, allowing closely compact strands
- quaternary with staggered ends
- covalent cross-links provide strength
- fibrils make up collagen fibres & are positioned in line with the forces they’re withstanding.
- STABLE: contains proline and hydroxyproline, which Rgroups repel each other.

Keratin:
- in hair nails, etc.
- contains cysteine w/ strong disulfide bridges, making it less flexible, hence why hair has less than nails

Elastin:
- elastic fibres e.g. skin, tissue, bone
- In blood vessels and alveoli, allowing them to expand and return to shape
- made of tropoelastin molecules (hydrophobic areas interact to form elastin)
- Structure stabilised by cross-linking involving lysine.

40
Q

What does a nucleotide consist of? (3)

A

phosphate group
ribose sugar
nitrogenous base

41
Q

what does DNA stand for?

A

deoxyribonucleic acid

42
Q

How are nucleotides joined to form polynucleotides? (3)

A
  • Nucleotides linked in a condensation reaction
  • 5’ carbon on ribose has phosphate that forms covalent bond with OH group on the 3’ carbon of an adjacent nucleotide.
  • This is a PHOSPHODIESTER BOND
43
Q

What are the four nucleotide bases in DNA and how do they differ from the 4 in RNA?

A

DNA:
Adenine
Thymine
Cytosine
Guanine

In RNA, the T is replaced by U, which is Uracil

44
Q

In DNA, which bases are the purines and which are pyrimidines? (2)

A

Purines = A & G (larger, double carbon ring)
Pyrimidines = T & C (smaller, single carbon ring)

45
Q

What are the differences between DNA & RNA? (6)

A

DNA:
- storage (stores genetic info needed by organism)
- ‘deoxy-‘ as 2nd carbon is attached to 2 hydrogens and no oxygen
- double helix held together by H-bonds between bases. each strand has a phosphate group (5’) and OH group (3’) at each end.
- Antiparallel as runs in opposite directions
- ACTG bases

RNA:
- Transport (transfer genetic info from DNA to proteins)
- Ribonucleic acid (no ‘deoxy’) as has an OH group on 2nd caron, unlike DNA.
- DNA too long to leave nucleus, so a short section is transcribed into mRNA.
- ACUG bases
-single strand, forms phosphodiester bonds like DNA. Leaves nucleus to ribosomes.

45
Q

Why is the DNA strand antiparallel?

A

1 stans begins from 5’ and the other begins from 3’, therefore they run in opposite directions.

46
Q

How many hydrogen bonds are there between the different purines and pyrimidines?

A

A-T & A-U have 2 H-bonds
C-G have 3 H-bonds

47
Q

How is DNA packaged in eukaryotes and prokaryotes? (4)

A

Eukaryotic:
-packaged in chromosomes in nucleus
-DNA tightly coiled and folded
-Histones (proteins) wrap around DNA to form chromatin, which makes chromosomes

Prokaryotic:
- DNA lose in cytoplasm
- No histones or chromosomes

48
Q

Why does DNA need to replicate? (2)

A
  • growth & repair of new tissues (produce 2 genetically identical daughter cells)
  • Reproduction - gametes need DNA to pass on genetic info
49
Q

What are the three types of DNA replication? (3)

A

-conservative: completely separate to parent strand
-semiconservative: half parent, half daughter strand
-dispersive: newly synthesised strands fused with original strands

50
Q

Describe the process of semi-conservative DNA replication. (4)

A

1) DNA helicase breaks H-bonds holding bases together, so DNA strands unwind.
2) Free nucleotides in the nucleus are attracted to unpaired complimentary bases
3) DNA polymerase joins nucleotides together & forms phosphodiester bonds for the sugar phosphate backbone. H-bonds reform between bases.
4) All nucleotides form polynucleotide chain.
5) Two identical DNA molecules formed half parent DNA, half new daughter DNA.

50
Q

What is a codon?

A
  • 3 bases = 1 amino acid
51
Q

Explain the process of DNA transcription

A

1) Helicase breaks hydrogen bonds between bases and unwinds section of DNA containing the gene.
2) sense strand has the code for protein synthesis, antisense strand is complimentary to the sense strand and acts as the template strand so that complimentary RNA has the same base sequence as the sense strand.
3) RNA polymerase runs along template strand and matches free RNA nucleotides when DNA unzips.
4) RNA nucleotides join and form pre-mRNA
5) When RNA polymerase reaches stop codon, chain is terminated and pre-mRNA detaches. mRNA travels to the ribosome (leaves through nuclear pore).

51
Q

Describe the process of DNA translation. (5)

A

1)mRNA combines with small subunit of ribosome
2) mRNA attaches to start codon AUG (methionine)
3) tRNA has complimentary anticodon (UAC) that binds to mRNA codon.
4) ribosome moves along mRNA, bringing 2 tRNA molecules in at a time.
5) amino acids on tRNA join by a peptide bond
6) first tRNA is released as ribosome moves along mRNA. second tRNA becomes the first.
7) Repeats until ribosome reaches stop codon & polypeptide chain is released.

52
Q

List the properties of ATP. (5)

A

small: easily move in & out cell

water soluble: energy-requiring processes happen in aqueous environment

Bonds between phosphates have immediate energy: useful as not too large that it wastes energy as heat.

Release energy in small quantities: suitable to cellular needs & energy not wasted as heat.

Easily regenerated: Can be recharged with energy

53
Q

How does ATP release energy?

A

Hydrolysis:
-Water added to remove last phosphate group
-ATP –> ADP + Pi
-Releases energy to be used by the cells
-Unstable phosphate bonds = only short-term storage, so can instantly release energy

54
Q

What is the test for a protein?

A
  • Biuret
    -Cu2+ in alkaline solution, usually copper sulphate and sodium hydroxide
  • colour change to violet