organic molecules

Question 1

condensation reactions

Answer 1

reactions between molecules that involve the loss of water molecules, forming more complex molecules

Question 2

glycosidic bonds

Answer 2

characteristics bonds between carbohydrates

Question 3

sorbitol

Answer 3

hydrogenated glucose (C6H14O6)

Question 4

oligosaccharides

Answer 4

carbohydrates with 3-10 sugar units

Question 5

amylopectin

Answer 5

branched polysaccharide that contain 1-4 and 1-6 glycosidic bonds

Question 6

glucose isomers

Answer 6

alpha-glucose and beta-glucose

Question 7

triglycerides

Answer 7

three fatty acid chains + glycerol (propane-1, 2,3-triol

Question 8

saturated fatty acids

Answer 8

compact fatty acids that have the maximum number of hydrogen atoms per carbon atom (c—c bonds only)

Question 9

unsaturated fatty acids

Answer 9

fatty acids that have one or more c=c double bond

Question 10

esterification

Answer 10

condensation reactions between fatty acid chains and glycerol

Question 11

kinks

Answer 11

bends caused by c=c double bonds in unsaturated fatty acids

Question 12

amino acids

Answer 12

building blocks of proteins

Question 13

structural and functional proteins

Answer 13

structural - simple proteins that make up structure of the body
functional - every other protein (used in metabolic reactions)

Question 14

peptide bonds

Answer 14

characteristic bond of animo acids - formed in condensation reactions

Question 15

where does formation of peptide bonds occur between

Answer 15

carboxyl and amino groups

Question 16

hydrogen bond

Answer 16

weak bonds between ∆+ hydrogen of the amino group and ∆- oxygen of the carboxyl group

Question 17

disulfide bridges/linkages

Answer 17

strong covalent bonds caused by oxidation of the sulfur-containing R-group of cysteine amino acids

Question 18

ionic bonds

Answer 18

bonds between strong opposite charges that involve the transfer of electrons

Question 19

hydrophobic interactions

Answer 19

attractive and intermolecular forces caused by interactions between hydrophobic substances

Question 20

primary structure

Answer 20

long linear polypeptide chains

Question 21

secondary structure

Answer 21

polypeptide chain that folds and coils into a-helix and b-pleated sheets held by hydrogen bonds

Question 22

tertiary structure

Answer 22

a-helix and b-pleated sheets fold into complex 3d shapes. held by hydrogen, disulfide, and ionic bonds between the R-groups

Question 23

quaternary structure

Answer 23

polypeptide chains bond to other polypeptide chains

Question 24

collagen

Answer 24

an insoluble fibrous protein made of three parallel polypeptide chains with occasional cross linkages tied into a helix, held by hydrogen bonds. used to form structures like skin, hair, and horns. (amino acids present: glycine, proline, hydroxy proline)

Question 25

LDL and HDL

Answer 25

LDL: low density lipoprotein (more lipid less protein) HDL: high density lipoprotein (less lipid more protein)

Question 26

colloid

Answer 26

microscopic particles remain suspended in a solution; solute doesn't completely dissolve.

Question 27

conjugate proteins

Answer 27

proteins conjugated to other prosthetic groups, like carbohydrates, lipids, or iron, to enhance the functions of the protein.

Question 28

fibrous protein

Answer 28

simple (little to no tertiary structure) insoluble proteins that have *tensile* strength. normally used to form structures

Question 29

globular proteins

Answer 29

glob-like proteins that are very *complex*, and so are not stable (eg: haemoglobin). they are water-soluble due to hydrophilic substances oj the surface

Question 30

haemoglobin

Answer 30

globular protein made of 4 polypeptide, each with one heme group, which can transport *one* molecule of oxygen each

Question 31

denaturation

Answer 31

a loss in the *3d shape* of a protein due to rise in temperature/pH, breaking down the hydrogen and disulfide bridges that hold the structure intact.

Question 32

why does the primary structure affect the tertiary/quaternary structures

Answer 32

polypeptides have different sequences of amino acids, which have different R-groups, and so disulfide, ionic, hydrophobic, and hydrogen bonds form in different places or some dont form at all

Question 33

sequence of forming collagen

Answer 33

3 polypeptide chains tightly wound and kept tight with h-bonds ==> collagen molecule ==> collagen fibril ==> collagen fibre

Question 34

why do unsaturated fatty acids have lower boiling points

Answer 34

presence of c=c double bond creates kinks, which prevents fatty acid from becoming compact. so there is more of it exposed, reducing the amount of heat needed to break bonds down.

Question 35

polysaccharide traits/adaptations

Answer 35

compact and insoluble so they don't hydrolyse easily insoluble so large quantities of polysaccharides in cells have no osmotic effect compact yet large enough so they cant diffuse out of cells inert so they dont participate in surrounding reactions, so they dont get used up