biology Flashcards
(65 cards)
what are glucose two isomers
alpha glucose and beta glucose
what is an isomer
molecules with the same molecular formula as each other but the atoms are connected to each other in a different way.
what is hydrolysis reaction
breaking chemical bonds of large molecules to smaller components by using water
amylose structure
long unbranched chain of alpha glucose. coil structure, compact and easy to store and fit into small spaces.
amylopectin structure
long branched chain of alpha glucose. side branches allow enzymes to get to the glycosidic bonds, glucose released quickly.
starch adaptations
starch is insoluble in water and doesn’t affect water potential because it doesn’t cause water to enter the cell by osmosis, which would make it swell.
cellulose structure.
made up of long , unbranched chains of beta glucose. when b glucose molecules bond they form straight cellulose chains. linked together by hydrogen bonds to form strong fibres called microfibers.
glycogen structure
long very branched chain., compact so good for storage.
what is a triglyceride made up of
3 fatty acids and 1 glycerol
how is a triglyceride formed.
a condensation reaction which is the removal of water.
reducing sugar
a sugar that can give electrons to other substances to reduce them, getting oxidised.
non reducing sugars
no free aldehyde so it cant act as a reducing agent
what are the 20 amino acids
alanine, arginine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, proline, serine, threonine, tryptophan, tyrosine, and valine
what are amino acids made up of
amino group, r group(side chains, variable), carboxylic group
what are phospholipids made up of
1 glycerol, 2 fatty acids, 1 phosphate group.
phosphate head
hydrophilic and polar
2 fatty acid tails
non polar, hydrophilic so face inwards.
R group
gives each amino acids its chemical properties
4 levels of protein formation
primary, secondary, tertiary, quaternary.
primary
order of amino acids, combinations and numbers, pleated sheets.
secondary
helix structure, can form because of hydrogen bonding’s.
tertiary
folds, twists and overlaps. now a protein
quaternary
proteins interacting, two or more chains .
induced model
active site changes shape as substrate binds. this distorts bond leading to a reaction to lower activation energy. some proteins change their shape (conformation)