when polymers are formed, it results in water being released (monomer to polymer)
hydrolysis reaction
when polymers split into shorter chains, they need the addition of water (polymer to monomer)
metabolism
the sum of all chemical reactions that take place in the body
monosaccherides
sweet tasting, soluble substance with formula (CH2O)n n=(3-7)
examples:
glucose
galactose
fructose
isomers
molecules with same molecular formula, but with atoms connected in a different way
a glucose
b glucose
disaccherides
glucose + glucose = maltose
glucose + fructose = sucrose
glucose + galactose = lactose
starch
a glucose monomers linked by glycosidic bonds, formed by condensation reaction
chain of a glucose wound into tight coil
found in plants as starch grains, in seeds and storage organs
insoluble - doesnt draw in water
compact - fits in small spaces
easily hydrolysed to a glucose, so can be used in respiration
glycogen
a glucose monomers
shorter chains, highly branched
easily hydrolysed due to shorter chains
cellulose
b glucose monomers
to form glycosidic bonds, each molecule is rotated 180 degrees compared to one next to it
straight, unbranched chains that run parallel
hydrogen bonds link chains to make it strong
good structual material
group to form microfibril fibres
prevent cells from bursting, so are turgid when full of water. helps support stems
main lipid groups
triglycerides
phospholipids
roles of lipids
phospholipids contribute to flexibility of membranes and transfer of lipid soluble substances across them.
source of energy
waterproofing
insulation
protection
lipids as source of energy
when oxidised, lipids provide over twice the energy as the same mass of carbohydrate
lipids for waterproofing
plants and insects have waxy, lipid cuticles that conserve water.
mammals produce an oily secretion from the sabaccous glands in the skin
lipids for insulation
slow heat conductors. stored beneath bpdy to retain heat. act as electrical inulators in myelin sheath around nerve cells
lipids for protection
fat often stored around delicate organs such as the kidney
properties of triglycerides
have 3 fatty acids combined with glycerol
each fatty acid forms an ester bond with glycerol in a condensation reaction
hydrolysis of triglyceride produces glycerol and 3 fatty acids
glycerol molecule in all triglycerides is the same
over 70 different fatty acids and all have a carboxyl group with hydrocarbon chain attatched
either saturated, monounsaturated or polyunsaturated
saturated fatty acid chain
no carbon-carbon double bonds
monounsaturated fatty acid chain
single double bond
polyunsaturated fatty acid chain
more than one double bond
structure of triglycerides
high ratio of energy storing carbon - hydrogen bonds to carbon atoms - good source of energy
low mass to energy ratio - good storage molecule as much energy can be stored in small volume
large, non-polar molecules so insolube in water. their storage doesnt affect osmosis in cells or their water potential
high ration of hydrogen to oxygen atoms, release water when oxidised
properties of phospholipids
one of fatty acid molecules replaced by phosphate molecule
hydrophilic
hydrophilic head - repels fat
hydrophobic tail - mixes reasily with fat
structure of phospholipids
polar - form bilayer within cell-surface membrane in an aqueous environment. a hydrophobic barrier form between inside and outside of cell
heads help to hold at surface of membrane
structure allows them to form glycolipids by combining with carbohydrates in membrane. important in cell recognition
lipids are stored in...
adipose tissue
lipids have...
ester bonds
properties of proteins
large molecules
vary in shape
enzymes (group of proteins) involved in almost every living process
structure of amino acid
basic monomer units. combine to make a polymer, polypeptide. polypeptides combine to form proteins. every amino acid has a central atom to which are attatched 4chemical groups:
amino group (-NH2)
carboxyl group (-COOH)
hydrogen atom (-H)
R group (different in every amino acid)
amino acidstructure
formation of peptide bond
amino acid monomers combine into dipeptide. bond forms between carboxyl group of one amino acid to the amino group of another in a condensation reaction between OH and H. bond can be broken by hydrolysis
primary structure of polypeptides
amino acid monomers joined through polymerisation (sequence of amino acids). forms chain called a polypeptide. forms primary structure of any protein.
sequence determined by DNA.limitless types of primary protein structure
structure determines shape, therefore the function
secondary structure of proteins
amino acids that make up polypeptide possess amino groups and carboxyl groups
hydrogen of amino group has positive charge, oxygen of carboxyl group has negative charge, so both readily form weak hydrogen bonds.
bonds cause the long peptide chain to be twisted into 3D shape (a-helix or b-sheet)
.
tertiary structure of proteins
interaction between R groups
structure maintained by different bonds, depending on primary structure of protein:
disulphide (covalent) bridges - fairly strong, not easily broken
ionic bonds - formed between any carboxyl and amino acid groups not involved in forming peptide bonds, easily broken by pH changes
hydrogen bonds - numerous, easily broken
quarternary structure of proteins
several polypeptide chains bonded together.
anabolic reactions
reactions that build up molecules
catabolic reaction
reactions that break down molecules
metabolic pathway
sequence of enzyme controlled reactions
specificity
only able to catalyse specific reaction
extracellular
an enzyme that is secreted by a cell and functions outside of that cell
intracellular
an enzyme that functions within the cell it was produced