Flashcards
Organic Chem: Macromolecules
Cards in this deck (19)
- 1PolymerA large molecule (macromolecule) consisting of smaller repeated units called monomers
e.g. natural - DNA, silk, cellulose
synthetic - Teflon, nylon, polyester - 2Addition polymerisationA double bond is broken in the monomer and the repeating units join to form a polymer
- 3Polymerisation of polyethene
- 4HDPEProperties:
- Long straight polymer chain with few side chains --> linear shape allows efficient packing of molecules, hence stronger dispersion forces
- Higher MP, stiff, rigid
Uses: food containers, pipes - 5LDPEProperties:
- Side chains prevent molecules from packing efficiently, hence weaker dispersion forces
- Amorphous (non-crystalline, irregular arrangement of molecules)
- Lower MP, soft, flexible, fairly weak
Uses: cling wrap, squeeze bottles, plastic bags - 6Polymerisation of polytetrafluroethene (Teflon)Properties: - chemically stable, low friction, water/oil repellent, high MP, high electrical resistance
Uses: non-stick coatings on cooking equipment, cable insulation
- 7Condensation polymerisationJoining of individual monomers by the elimination of small molecules like H2O or CO2
- 8Polyesters- H atom of diol and and OH atom of dicarboxylic acid combine to form water, and remaining parts join via ester groups
- Permanent net dipole exists around each of ester group --> DP-DP, dispersion forces
- High degree of crystallinity, high strength and resistance to creasing/wrinkling - 9Polyethylene terephthalate (PET)Uses: soft drink bottles, food jars
- 10Polyamides- H atom of diamine and OH atom of dicarboxylic acid combine to form water, and remaining parts join via ester groups
- H-bonds can form between lone pair of electrons on the O atom (-C=O group) of one molecule and a H atom (N-H group) of another
- High tensile strength and stiffness - 11Nylon 6,6Uses: clothing, stockings, fishing line, rope
- 12PolypeptideA polymer chain of α-amino acids, formed during a condensation reaction (-COOH and -NH2 groups join by elimination of water)
- Dipeptide has 2 α-amino acid residues
- Tripeptide has 3 α-amino acid residues - 13Protein- A peptide chain consisting of at least 50 α-amino acid residues
- Important molecular substances found in all living things e.g. keratin forms hair/skin fingernails, haemoglobin carries oxygen in the blood - 14Peptide bond vs linkagePeptide linkage - refers to the functional groups that link the monomers along a peptide chain (CONH)
Peptide bond - covalent bond between consecutive amino acid monomers along a peptide chain (C-N) - 15Primary structureRefers to linear sequence of α-amino acid residues
- When naming, start at the N-terminus (NH2) and finish at the C-terminus (COOH) e.g. Ala-Gly is different from Gly-Ala - 16Secondary structure- Refers to regular arrangement of various sections of the protein chain (only protein backbone is involved)
- Results from H-bonding between N atom of amide (-N-H) group and O atom of carbonyl (-C=O) group - 17α-helix- Coiling of amino acid strands
- H-bonding occurs within peptide chain
- Amide group must be situated four residues further along the spiral from the carbonyl group
- 18β-pleated sheets- Twisting of polypeptide chains around one another
- H-bonding occurs between adjacent polypeptide chains
- Occur with small side chains of α-amino acid residues
- 19Tertiary structure- Overall 3D shape that forms due to main chain folding and bonding back on itself
- Various bonds form between the residue side chains e.g. disulfide bridges, H-bonds, DP-DP, dispersion forces and ionic bonds
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- Description
- Proteins, polypeptides, polymerisation, primary/secondary/tertiary structure
- Created by
- Mel M
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