biological molecules Flashcards
describe covalent bonds
atoms share electrons
what do carbs contain
carbon
hydrogen
oxygen
name 3 monosaccharides
lactose
sucrose
glucose
name 3 polysaccharides
cellulose
starch
glycogen
glucose:
polar?
soluble?
polar+ soluble
bonds in amylose
I-4
glycosidic
form long twisted chain
bonds in amylopectin
1-4/1-6
glycosidic
form branched structure
bonds in cellulose
hydrogen bonds
what types of sugars are reducing sugars
all monosaccharides
some disaccharides
can donate electrons
how to test for non-reducing sugars
Benedict’s test
boil with hydrochloric acid
sugars hydrolysed
iodine test
what for?
how?
starch
few drops of iodine dissolved in potassium iodide solution
lipids
polar?
soluble?
not polar/ soluble
double chain is ……. fatty acids
unsaturated
liquids
identification of lipids
emulsion test
sample mixed with ethanol
solutions mixed with water
white emulsions= lipids
role of lipids
membrane formation hormone production electrical/ thermal insulation buoyancy protection of vital organs
3 types of lipid
triglyceride
- 1 glycerol + 3 fatty acids
- ester bonds between mol.s
phospholipid
- modified triglycerides
- fatty acid chain replaced with a phosphate group
sterol
-4 carbon ring structure
what enzyme catalyses the reaction of peptides =>amino acids
protease
bonds in primary protein structure
peptide
bonds in secondary protein structure
hydrogen bonds
bonds in tertiary (and quaternary) protein structure
hydrophobic + hydrophilic interactions
disulphide bonds
ionic bonds
hydrogen bonds
what bond is formed during condensation reaction
glycosidic
between carbons 1 and 4
how are amino acids joined
hydroxyl in carboxyl group reacts with amine group of another
peptide bonds
condensation reaction
forms polypeptide
name + describe types of proteins
globular
- water soluble
- proteins in tertiary structure
- regulate processes necessary for life
- e.g. insulin (hormone)
conjugated
- globular protein with non-protein prosthetic group
- lipids + carbs combine with proteins to form lipoproteins and glycoproteins
- e.g. catalase (enzyme)
fibrous
- many amino acids with hydrophobic r groups in primary structure
- make long strong mol.s NOT folded into complex 3D shapes
- e.g. keratin, elastin, collagen