2.3 Biological Molecules (Spec) Flashcards
Biochemical molecules
Carbon Nitrogen Hydrogen Oxygen Sulfur Sodium Potassium Iron
Ca2+ function
Nerve impulse transmission, muscle contraction
Glycosidic bond formation/breakage
Monosaccharide -> Disaccharide/Polysaccharide
Condensation reaction
Polysaccharide/Disaccharide -> Monosaccharide
Hydrolysis reaction
Hydrogen bond formation (Water)
Affinity to shared pair of electrons in covalent bond
Oxygen > Hydrogen
Partial positive on oxygen, partial negative on hydrogen
Electrostatic attraction between lone pair on O and partial positive on H of different molecules
High boiling point function in water
Coolant - Narrow temperature range of enzyme activity
Density function
Ice < Water
Insulating layer for lakes/ponds
Creation of semi-aquatic habitat
Na+ function
Nerve impulse transmission, kidney function
K+ function
Nerve impulse transmission, stomatal opening
H+ function
Catalysis, pH determination
NH4+ function
Bacterial NO3- production
NO3- function
Plant amino acid & protein formation (N)
HCO3- function
Blood pH maintenance
Cl- function
Cell pH maintenance (Na+/K+)
(PO4)3- function
Bone, cell membrane, nucleic acid & ATP formation
OH- function
Catalysis, pH determination
Cohesion function in water
Transport medium
Adhesion function in water
Capillary action
Polarity function in water
Universal solvent
Starch structure & function
20-30% amylose
70-80% amylopectin
Dense energy storage
Water-insoluble
Amylose structure
Alpha-glucose polymer
1-4 glycosidic bonds
Straight chain -> helical structure
Amylopectin structure
Alpha-glucose polymer
1-4 & 1-6 glycosidic bonds
Highly branched structure
Dense energy storage
Glycogen (properties, structure, function)
Water-insoluble Alpha-glucose polymer 1-4 & 1-6 glycosidic bonds Highly branched structure Dense energy storage - animals' high metabolic demand
Cellulose
Water-insoluble
Beta-glucose polymer
Alternate monomers rotated 180 degrees
1-4 glycosidic bonds form on opposite chain sides
High compressive strength
Hydrogen bonds - chains, microfibril, macrofibril
Benedict’s test
For reducing sugars Equal volume of solution and sample Heat in water bath CuSO4 & NaOH solution Blue - Negative test Green - Low reducing sugar conc Yellow/Orange - Medium reducing sugar conc Red - High reducing sugar conc
Iodine test
For starch
Equal volume of solution and sample
Negative test - orange
Positive test - blue-black
Reagent test strips
Colour-coded chart - reducing sugar conc
Industrially manufactured
Triglyceride structure/formation
3 fatty acid chains Glycerol backbone Ester bonds between fatty acid chain & backbone Ester bond formed in condensation Ester bond broken in hydrolysis
Triglyceride function
Long-term energy storage
Thermal insulation -> reduce heat loss
Cushioning protection of vital organs
Aquatic animals’ buoyancy
Phospholipid structure, function, properties
Hydrophilic phosphate head (Inorganic phosphate group)
Hydrophobic fatty acid tails (hydrocarbon chain ending in methyl group)
Phospholipid bilayer - plasma membrane
Ester bond between glycerol & fatty acid chain, glycerol & phosphate head
Cholesterol function
Stability to cell membrane
Regulates membrane fluidity
Emulsion test
For lipids Equal volume of ethanol, sample & distilled water Shaken, not stirred Milky emulsion - positive test Clear solution - negative test
Amino acid structure
Amine group, R-group, carboxyl group
Dipeptide/Polypeptide formation/breakdown
Peptide bond (C-N) forms in condensation reaction
Hydroxyl of carboxyl on one amino acid
Hydrogen of amine of another amino acid
Catalysed by peptidyl transferase - present in ribosomes
Hydrolysis reverse reaction
Catalysed by protease enzymes
Primary protein structure
Peptide bonds
Order of amino acids
Secondary protein structure
Hydrogen bonds within polypeptide chain
Alpha helix/Beta pleated sheet dependent on primary structure
Tertiary protein structure
Ionic bonds Hydrogen bonds Disulfide bridges Hydrophobic/Hydrophilic interactions Within polypeptide chain, between R-groups
Quaternary protein structure
Ionic bonds Hydrogen bonds Disulfide bridges Hydrophobic/Hydrophilic interactions Between subunits/polypeptide chains
Biuret test
For proteins Equal volume of solution and sample CuSO4 & KOH solution Blue solution - negative test Lilac solution - positive test
Nucleotide structure
Pentose sugar Phosphate group Nitrogenous base DNA - Deoxyribose, phosphate & A, T, C or G RNA - Ribose, phosphate & A, U, C or G
Polynucleotide formation
Phosphodiester bond formed between 3’ hydroxyl and 5’ phosphate of adjacent nucleotides
Catalysed by DNA/RNA polymerase
Formed in condensation reaction/broken by hydrolysis
DNA structure
Sugar phosphate backbone (Deoxyribose and phosphate)
Phosphodiester bonds between 3’ hydroxyl and 5’ phosphate
Nitrogenous bases attached to C1 of deoxyribose
Hydrogen bonds between complementary nitrogenous base pairs
Pyrimidines always pair with purines (A-T and C-G)
DNA purification
Grind cells in pestle and mortar - break cell walls (plant-cellulose, bacterial-peptidoglycan, etc)
Add detergent - break membranes, release cell contents into solution
Add salt - breaks hydrogen bonds -> DNA & water
Add protease-break down histones associated w/ DNA
Add ethanol down test tube side to prevent agitation and allow DNA to precipitate
DNA replication
- DNA helicase breaks hydrogen bonds between bases, unwinds & unzips the DNA double helix
- Free DNA nucleotides arrange by complementary base pairing and form hydrogen bonds with exposed bases of existing strands
- DNA polymerase catalyses formation of phosphodiester bonds between free DNA nucleotides in condensation (3’ hydroxyl/5’ phosphate)
Each daughter DNA molecule has one old strand and one new strand
Genetic code nature
Non-overlapping: Each codon is read individually
Triplet code: Three-base sequence codes for one amino acid
Universal: Same codons code for same amino acids in all organisms
Degenerate: >1 codon codes for each amino acid
DNA transcription (protein synthesis)
DNA helicase breaks hydrogen bonds between bases in DNA at locus of gene coding for desired protein
Free RNA nucleotides arrange by complementary base pairing to exposed template strand (complementary-template, identical-coding), form hydrogen bonds w/ template strand
RNA polymerase catalyses phosphodiester bond formation between RNA nucleotides
Pre-mRNA matures as introns removed by enzyme (introns: non-coding)
mRNA leaves nucleus by nuclear pore
DNA translation (protein synthesis)
mRNA moves to ribosome
mRNA passes between ribosomal subunits
tRNA molecules w/ complementary anticodons to mRNA codons enter ribosome and form hydrogen bonds
2 tRNA molecules can enter ribosome at any time
tRNA carries specific amino acid, peptide bond formed between amino acids, catalysed by peptidyl transferase
tRNA w/ complementary anticodons continue to bring amino acids to ribosome until stop codon reached - no amino acid on stop codon - polypeptide released.
ATP structure
Nucleotide derivative:
Ribose, adenine and phosphate groups
AMP: Adenosine monophosphate (1 phosphate)
ADP: Adenosine diphosphate (2 phosphates)
ATP: Adenosine triphosphate (3 phosphates)
Most energy stored in final phosphate bond in chain
Inorganic phosphates added in condensation/removed in hydrolysis