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benedicts test for reducing sugars
add equal volumes of sugar sample and add benedicts reagent. heat the mixture in water bath for 5 mins. brick red precipitate will form
what is a reducing sugar
a sugar that can reduce (give electrons to) another chemical
benedicts test for non reducing sugars
with food sample, add an equal volume of dilute hydrochloric acid in a test tube in water bath for 5 mins. add sodium hydrogen carbonate solution. heat resulting solution with an equal volume of benedicts solution for 5 mins. turns orange brown
what does dilute hydrochloric acid do in the benedicts test for non reducing sugars
it hydrolyses any disaccharide into monosaccharides, thus also forming reducing sugars
structure of starch
amylopectin- branched chains of alpha glucose, 1-4 glycosidic bonds and 1-6, creating branches.
amylose- linear, unbranched chain by 1-4 glycosidic bonds, forms a coiled helical structure
purpose the structure of amylose serves
makes the molecule compact so stored easily
purpose of structure of amylopectin
larger SA for enzymes to work on, thus glucose molecules can be released much quicker rate
structure of starch related to its function
- starch insoluble so doesnt affect wp
- large enough that it doesnt diffuse out of cells
- compact enough so that alot of it can be stored in a small space
- branched- each end can simultaneously be acted on by enzymes, so glucose is quickly released
structure of glycogen related to its function
- insoluble- no effect on water potential of cell
- insoluble- so doesnt diffuse out of cells
- compact- alot of it can be stored in a small space
- very highly branched- each end can simultaneously be acted on by enzymes, so glucose is quickly released.
why do animals need highly branched glycogen
because animals metabolic rate is faster than plants and so needs glucose to be released quicker.
structure of cellulose
made up of straight chains of beta glucose. chains parallel to each other, so H bonds form cross-linkages. all the H bonds together strengthens the cellulose. forms microfibrils
how the structure of triglycerides relate to their properties
- triglycerides have a high ratio of energy-storing carbon-hydrogen bonds to carbon atoms, so its a good source of energy.
- low mass to energy ratio, so theyre good energy storage molecules.
- large and non polar, therefore insoluble, therefore doesnt affect osmosis
- high ratio of hydrogen to oxygen atoms, so can release water when oxidised, hence provide a source of water
roles of lipids
source of energy
waterproofing
insulation
protection
structure of phospholipid and relation to properties
- polar, therefore will position itself to form a bilayer
- the structure allows them to form glycolipids by combining with carbohydrates within the CSM. these are important in cell recognition
primary sequence of a protein
unique sequence of amino acids that make up a protein or polypeptide chain
secondary sequence of protein
way in which the primary structure of a polypeptide chain folds e.g. alpha helix or beta pleated sheets. shape is help by H bonds
tertiary sequence of protein
overall 3D structure of protein, held together by H bonds and iconic bonds and disulfide bridges
quaternary sequence of protein
if a protein is made up of several polypeptide chains that are linked in various ways, the way they are arranged is called the quaternary structure
test for proteins
add equal volumes of sample and sodium hydroxide to a test tube. add a few drops of dilute copper II sulfate and mix. if purple solution if protein is present. peptide bonds broken
what are fiberous proteins made up of
made of long molecules arranged to form fibres. several helices may be wound around each other to form very strong fibres
what are globular proteins made up of
made of chains folded into a compact structure. one of the most important classes are the enzymes. although, these folds are less regular than in a helix, they are highly specific and particular protein will always be folded in the same way.
what is Hb made of
two alpha polypeptide chains
two beta polypeptide chains
an inorganic haem group Fe2+
collagen structure
three polypeptide chains wound around each other
each of the three chains is a coil itself.
hydrogen bonds form between these coils
collagen molecules form further chains with other collagen molecules and form covalent cross links with each other, which are staggered along the molecules to further increase stability. collagen molecules wrapped around each other form collagen fibrils which themselves form collagen fibres
functions of collagen
form structure of bones
makes up cartilage and connective tissue
prevents blood that is being pumped at high pressure from bursting the walls of arteries