B1 form and function of molecules Flashcards
Polymer
definition
a chain of repearting monomers
umbrellar term for polysaccharides and polypeptides
monomer
definition
the building blocks of macromolecules
polysaccharide
definition
many monosaccharides chemically bonded together for energy storage
monosaccharide
definition
one sugar units that are the monomers of carbohydrates
can be pentose or hexose
polypeptide
definition
a series of amino acids chemically bonded together
condensation reaction
explain
joins monosaccharides together to form polysaccharides by removing the H from one and the OH from another to form a waste product of water
Monosaccharides (glucose) are the monomers of…….
carbohydrates
fatty acids and glycorol/phosphates are the monomers of……
lipids
amino acids are the monomers of……
proteins
nucleotides are the monomers of……..
nucleic acids
properties of glucose
4 total
contains 5 polar OH groups therefore the whole molecule is polar
1. molecular stability
(due to covalent bonds)
2. high solubility in water
(due to polarity)
3. easily transported
(due to solubility)
4. yields high energy when oxidised
(breaks high energy covalent bonds)
what are the 4 macromolecules
carbohydrates
lipids
proteins
nucleic acids
hydrolysis
explain
turns polymers into monomers by using water to add a H to one monomer and OH to another monomer breaking the bond and both monomers have another hydroxyl group
Amino acids contain
structure
- central carbon
- amine group (NH2)
- carboxyl group (COOH)
- unique R group
Condensation of amino acids into (dipeptides/proteins)
the H from the amine group of one amino acid is remove and the OH from the carboxyl group of another to from a peptide bond and water
peptide bond
explain
the strong covalent bond that forms when two amino acids bond together
Elements in Carbohydrates
Carbon, hydrogen, oxygen (1:2:1)
Elements in lipids
Long carbon hydrogen chains and a small amount of oxygen
Elements in proteins
Carbon, Hydrogen, oxygen and nitrogen
Starch (amylose and amelopectin) are examples of…….
carbohydrates
glycogen is an example of……
a carbohydrate
cellulose is an example of……
a carbohydrate
Saturated fatty acids contain…..
single carbon to carbon bonds
properties of saturated fatty acids
- densly packed
- high melting point so solid at room temp
monounsaturated fatty acids contain……
one double carbon to carbon bond, the rest are single
polyunsaturated fatty acids contain….
more than one double carbon to carbon bond
properties of monounsaturated fats
- less dense
- low melting point so liquid at room temp
what makes up a triglyceride
a glycerol backbone and three fatty acid tails joined by esther linkages (condensation reaction)
triglycerides are examples of……
lipids
properties of triglycerides
- non-polar
- hydrophobic
- stable energy storage
- contain lots of energy
- poor heat conductors so good insulation
phospholipids are an example of…..
lipids
properties of phospholipids
- contain 1 glycerol, 2 fatty acids and 1 phosphate group
- amphipathic (non-polar and polar regions)
steroids are an example of…..
lipids
properties of steroids
- made of 4 fused carbon hydrogen rings
how many amino acids are there
20 unique 9 are essential
amino acids contain….
an amine group, an R group and a carboxyl group
R groups can be…..
polar, non-polar and charged
what bonds to amino acids form firectly between eachother
peptide bonds
collagen is an example of…..
a protein
properties of collagen
- 3 polypeptide chains
- fibrous
- used for tendons and ligaments
insulin is an example of…..
a protein
properties of insulin
- globular
- non-conjugated
- 2 polupeptide chains attached by disulfide bridges
haemoglobin is an example of…..
a protein
properties of haemoglobin
- globular
- conjugated
- 4 polypeptides (2 alpha globin, 2 beta globin)
- 4 heme groups
What is the primary structure of a protein
the specific sequence of amino acids held together by strong peptide bonds
determined by DNA sequences
what can alter primary structure?
mutation
what is the secondary structure of a protein?
hydrigen bonds between the c and o, and n and h of two amino acids as they are charged
what alters secondary structure
bonds break in extreme environments
what is the tertiary structure of a protein?
the unique folding created by R group interactions
types of r group interactions
- disulfide bridges between cycstines
- ionic bonds
- hydrogen bonds
- hydrophibic interactions
what can break tertiary structure?
- mutations if they change the r groups
- denaturation in extreme temps
what is the quaternery structure of a protein?
the coming together or many polypeptides (non-conjugated) and non protein parts (conjugated) by r group interactions
changes to shape same as for teriary
Anabolic reaction
when two or more substrates form one product
e.g. photosynthesis
catabolic reaction
one substrate breaks down to form two or more products
e.g. digestion
