3.1 biological molecules Flashcards
what are monomers and polymers?
monomer- small basic molecular unit that forms polymers. e.g. monosaccharides, amino acids and nucleotides.
polymer- large complex molecule composed of long chains of monomers joined by covalent bonds
what are the types of reactions?
types of reactions
condensation reaction- makes polymers and forms a chemical bond between monomers, releasing a molecule of water.
hydrolysis reaction- breaks polymers by breaking the chemical bonds using a molecule of water.
what are carbohydrates?
all contain carbon, hydrogen and oxygen.
monomer is monosaccharides e.g. glucose, fructose and galactose
glucose is a hexose sugar- a monosaccharide with 6 carbon atoms in each molecule. there are 2 types of glucose- alpha and beta. is also an isomer.
what are disaccharides?
disaccharides form when 2 monosaccharides join together by condensation reactions.
glycosidic bonds form between 2 monosaccharides as a molecule of water is released e.g. starch
what is starch?
cells get energy from glucose, plants store excess glucose as starch
mixture of 2 polysaccharides of alpha-glucose.
what makes up starch?
amylose- long unbranched chain. angles of the glycosidic bonds give it a coiled structure, like a cylinder. compact and good for storage. 1,4-glycosidic bonds.
amylopectin- long branched chain. side branches allow enzymes that break down the molecule to break the glycosidic bonds easily, meaning that glucose can be released quickly. 1,4 and 1,6-glycosidic bonds
what is glycogen?
animals store exess glucose as glycogen.
alpha-glucose.
structure is similar to amylopectin but has more branches coming off it and so stored glucose can be released quickly.
compact.
1,4 and 1,6 glycosidic bonds
what is cellulose?
long unbranched chain of beta-glucose
when beta-glucose molecules bond, the form straight cellulose chains. chains are linked by hydrogen bonds to form strong fibres called microfibrils and means cellulose gives structural support
1,4 glycosidic bonds
what is the characteristics of lipids?
2 main types- triglyceride and phospholipid mainly oxygen, carbon and hydrogen large complex (macromolecule) not polymers non-polar wont dissolve in water
what are triglycerides?
good energy source
1 molecule of glycerol and 3 fatty acids
ester bonds form via condensation reactions
what are phospholipids and what do they make up?
make up the bilayer of membrane
head is hydrophillic and tail is hydrophobic, so form a double layer with head facing out.
has 2 fatty acids, a glycerol and a phosphate group
what are proteins?
monomer- amino acid
2 monomer- dipeptide
2 or more monomer- polypeptide
polymer- protein
how is an amino acid made up
NH2 is the amine group. COOH is a carboxyl group and R is a side chain.
all 20 amino acids only differ in their R group
what is the primary structure of proteins
sequence of amino acids found in polypeptide chains. sequence determines shape and function
what is the secondary structure of proteins?
shape polypeptides form as a result of hydrogen bonds
what is the tertiary structure of proteins
shape is due to bending and twisting. held together by bonds between R groups. hydrogen bonds between polar R groups, ionic between + and - charged R groups and disulphide links between sulphur atoms on the R groups
what is the quaternary structure of proteins?
same as tertiary but between 2 polypeptides
what is enzymes?
the tertiary structure of an enzyme may be altered by changes in pH or temperature.
catalyse metabolic reactions i.e. respiration and digestion
involved in the production of collagen
how do enzymes work?
speed up chemical reactions by acting as a biological catalyst
have an active site that is complementary to a specific substrate and are highly specific due to tertiary structure.
enzyme-substrate complex is what lowers the activation energy
lock and key model
induced fit model
what are competitive and non-competitive inhibitors?
competitive inhibitors- similar shape to the substrate and so compete with the substrate to bind to the active site but no reaction occurs.
non-competitive inhibitors- doesn’t bind to active sites and bind away from the active site but still changes the shape
what is the effect of temperature on enzymes?
As temp increases, the enzyme-controlled reaction will speed up.More heat means more kinetic energy, which increases collisions.The energy of collisions also increases, so each collision is more likely to result in a reaction.
what happens to enzymes if the temperature gets too high?
If temperature getstoohigh, enzymes vibrate more and as the temperature goes above a certain temperature, the vibrations breaks some of the bonds that hold the enzymes in place
The active site changes shape and the enzyme is denatured and no longer functions as a catalyst.