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how does the body regulate blood glucose levels?
hormones including glucagon, insulin, norepinephrine (adrenaline)
what is diabetes?
lacking ability to synthesis insulin and therefore unable to control blood sugar levels
what type of bond does glycogen contain
alpha 1,4- glycosidic linkages and alpha 1,6- linkages forming side branches
what is the importance of the bonds in glycogen
maximises the number of ends available for digestion by enzymes that catalyse the breakdown of glycogen, more free ends=faster synthesis/break down
what is the difference in cellulose bonds
it uses beta 1,4- glycosidic linkages which humans are unable to break down
what is an epimer of glucose and how does it differ
galactose, identical except for H and OH groups on C4 rotates 180 degrees
what is the difference in energy released by the monosaccharides glucose, fructose and galactose
none only the pathways differ
when does the body use fats for energy
when the supply of glucose decreases due to dieting, starvation or extended period between eating
how is palmitic acid composed
16 carbons with a carboxyl group at one end with a long hydrocarbon chain
what is a saturated fatty acid
fatty acid chain with no double bonds- all carbons are saturated with hydrogen atoms
what is the difference between fats, oils and waxes
composition of the molecules and degree of saturation
why are fatty acids an efficient form of storing energy
molecule is highly reduced, light-less dense than water, hydrophobic- doesn't need to be dissolved in water for storage, completely oxidised to form Co2 doesn't form toxic products
what functions do proteins serve
enzymes, transport (haemoglobin), storage, movement, structure, signalling (insulin, glucagon), regulatory, protective (immunoglobulins, antibodies)
what are the non polar amino acids
leucine, proline, mehtionine, tryptophan, isoleucine, phenylalanine, valine, alanine
what are the polar uncharged amino acids
glycine, serene, threonine, cysteine, asparagine, glutamine, tyrosine
what is the tertiary structure of proteins
shape of protein when alpha helices and beta sheets coil up and form a 3D structure, interactions of secondary structure with surrounding media
do all proteins possess quaternary structure
no but some proteins do not function without interacting with another identical protein
what is a homodimeric protein and example
2 interacting subunits of the same protein, alcohol dehydrogenase
how do pyrimidines and purines differ in structure
pyrimidines are composed of single hexagonal ring, purines are double rings
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