molecular building blocks Flashcards
macromolecules
simple molecules can form complex, large molecules. They can have osmotic, structural, optic, enzymatic and other complex functions. They are very heterogeneous. E.g. Haemoglobin, DNA
water
universal solvent, polarity, hydrogen bonding, liquid over a range of 0-100◦C, achieves maximum density at 4◦C. Excellent at dissolving ionic and polar compounds.
Water doesn’t interact with non-polar substances, lipids, aromatic groups and hydrophobic compounds
hydrogen bond
electronegative atoms such as oxygen, nitrogen can attract hydrogen atoms from other molecules, partial sharing of proton leads to an attraction, weak, responsible for unusual properties of H2O.
carbohydrates
- Cn(H2O)n
- Monosaccharide, disaccharides ect.
- Monosaccharide – chain of carbons, hydroxyl groups, one carbonyl group
- Cyclized (ring) structures- by the reaction of the aldehyde or ketone group with a hydroxyl group of the same molecule
- Sugar derivative – aminosugars (contain amino group), alcohol-sugars, phosphorylated, sulphated
- Glycosidic bond- hydroxyl group of a monosaccharide can react with an OH or an NH group to form glycosides (O-glycosidic bonds form disaccharides, N-glycosidic bonds are found in nucleotides and DNA)
- polysaccharides – starch, glycogen, proteoglycans (long, unbranched PS radiating from a core protein)
- Sulphated (glycosaminoglycans): sulphate groups e.g. heparin
lipids
- Straight C chains with a methyl group and a carboxyl group at the ends
- Melting point decreases with a degree of unsaturation (fluidity)
- Can be saturated or unsaturated
- Phosphoacylglycerols: derived from phosphatidic acid. Formed from fatty acids esterified to glycerol and phosphorylated
- Sphingolipids: derive from ceramide
nucleotides
- Nitrogenous base + sugar + phosphate
- Ester bond
- Nucleotide polymers can form using phosphodiester bonds
Eicosanoids
synthesised from 20 C atoms (cause inflammation)
amino acids
- Building blocks of proteins (20)
- Carbon with amino group, carboxyl group and side chain (R)
- Charge is determined by all three components
- Changes with the pH of the environment
- Side chain often determines polarity (hydrophilicity) or nonpolarity (hydrophobicity)
- Dissociation of amino groups – at different pH carboxyl and amino groups are ionised, some amino acids also have ionisable side chains
- Can be charged, neutral, aromatic
- Peptide bond – proteins are formed by aa linked by peptide bonds. Linear chains fold into different shapes to form 3D structures. Folding is determined by charged interactions, flexibility, and physical dimensions
- Proteins have structure-function relationship