Biomols Flashcards
(10 cards)
Starch and glycogen structure
-Helical/branched so compact and lots of ends to release glucose more quickly
-large so can’t leave cell
-insoluble so no osmotic effect
-1-6 glycosidic bonds
Cellulose structure
-polymer of beta glucose
-straight unbranched chain to provide strength collectively
-1-4 glycosidic bonds
-chains of cellulose bundle further into macro fibrils
-bundle further into macro fibres
Primary protein structure
-Sequence of amino acids in polypeptide chain
- peptide bonds
Secondary protein structure
-alpha helix coiling and beta sheet
-pleating of polypeptide chain
-H bonding between peptide bonds of diff amino acids
Tertiary protein structure
-overall structure of a polypeptide 3D
-4 bonding
H bonds, disulphide bridges, ionic
Quaternary protein structure
-overall 3D shape of a protein
-more than one polypeptide chain
Water property
-high specific heat capacity acts as a temp buffer
-high latent heat of vaporisation acts as a coolant
- cohesive creates a continuous water column
-polar solvent dissolves polar solutions to make polar solutions
Why ATP is a good energy source
-energy released in one reaction so is fast
-energy release in small amounts so prevents cell damage
-ATP is water-soluble so found in cytoplasm or CSM
DNA VS RNA
-double vs single stranded
-in the nucleus vs cytoplasm
-deoxyribose vs ribose
-longer vs shorter
-thymine vs uracil
-synthesised 1 vs many
-both have phosphodiester bonds
-
Translation
-mRNA attaches to ribosome
-Codon on mRNA binds to anticodon on tRNA
-tRNA brings specific amino acid
-amino acid joins by condensation reactions with peptide bonding using ATP
-tRNA release and ribosome moves along mRNA to form polypeptide