biological molecules part 1 Flashcards
what is a fancy name for a carbohydrate group
saccharide
what is a monomer
single molecules
what is a polymer
more than one monomer joined tog
what are monosaccharides
monomers
what does monosaccharides contain
Carbon
Hydrogen
Oxygen
what is the chemical formula of monosaccharides
(CH 0)
2 n
what is the function of monosaccharides
building blocks for larger mols
mono with 3 carbon name
triose
mono with 4 carbon name
tetrose
mono with 5 carbon name
pentose
mono with 6 carbon name
hexose
mono with 7 carbon name
heptose
what is the example of triose
glyceraldehyde
what is glyceraldehyde
used as intermediate during resperation reaction to release energy
what is the glyceraldehyde formula looking
3 C’s
what pentose sugar is in RNA
ribose
what pentose sugar is in DNA
deoxyribose
how to recognise ribose
has 2 OH
how to recognise deoxyribose
has 1 OH
what are the 3 monosaccharides you have to learn
glucose
fructose
galactose
what is the disaccharide formula
C H O
12 22 11
what is maltose made of
alpha glucose + alpha glucose
what is sucrose made of
alpha glucose + fructose
what is lactose made of
alpha glucose + galactose
what bonding is maltose
alpha 1 - 4 glycosidic bond
what bonding is sucrose
alpha 1-4 glycosidic bond
what bond is in lactose
beta 1-4 glycosidic bond
what reaction bonds 2 monosaccharides together
condensation reaction
condensation reaction defenition
bond that releases a molecule of water
defenition of polysaccharides
long chains of monosaccharides joined together by glycosidic bonds
what is cellulose
structural component of plant cell walls
what is startch
storage mol in plants
what is glycogen
storage mol in animals
what bonds are in cellulose
beta 1-4 glycosidic bonds
structure of amylose
straight chain of alpha 1-4
structure of amylopectin
branched 1-4 and 1-6
structure of glycogen
alpha branched 1-4 and 1-6
function of cellulose
strenght + support
how does structure of cellulose relate to function
straight chains = strong and rigid
function of startch
storage of glucose in plants
how does startch structure relate to function
fits in smaller spaces
insoluble so doesnt effect osmosis
function of glycogen
storage of glucose in animals
how does glycogen structure relate to function
branches - fits in a smaller space / area
what are oligosaccharides
3-9 monomers joined tog
what is glycogenesis
glucose makes glycogen
how to recognise fructose
extra CH2OH because fructose is fancy
how to recognise galactose
OH group at the top (on normal glucose its at the bottom)
what are the components of lipids
fatty acids + glycerol
what are the 4 roles of lipids?
source of energy
waterproofing
protection
insulation
what is the significance of lipids and waterproofing?
insoluble in water - preserves water
what is the significance of lipids and protection
stored around delicate organs such as kidney
what is the significance of lipids and insulation
slow conductors of heat - store body heat
what is an example of an insulation that lipids do?
electrical insulation
electrical insulation in lipids
myelin sheath around nerve cells
what is the significance of lipids and source of energy
when oxidised provides x2 energy comparded to carbohydrates
what are hydrophobic
cannot interact with water
what are hydrophilic
can interact with water
what is in lipids
C H O
solubility of lipids
insoluble in water
what are triglycerides made of?
glycerol
3 fatty acids
bonds in lipids
ester bonds
what do all fatty acids have at end of fatty acid chain
carboxyl group
what is a saturated lipid?
middle line (C) has no double bond
what is a monounsaturated lipid
middle line (C) has one double bond
what is a polyunsaturated lipid
middle line (C) has more than one double bond
whats in a phospholipid
phosphate head
glycerol
2 fatty acid tails
what bit of phospholipid is hydrophobic?
head
what bit of phospholipid is hydrophiliic?
tail
where are phospholipids
in cell membrane
which way does the hydrophilic heads face
out to water
what way does hydrophobic tail point
inwards
what are steriods
signalling mols
structure of steroids
4 carbon rings
where are steroids found?
cell surface membranes
whats the example of steroid we need to learn
cholesterol
how many different types of amino acids are there?
20
5 bits of a protien
amino group
central C
H
R group
Carboxyl group
what bonds do proteins have
peptide
what does the way the polypeptide bends depend on
R groups as Rs are attracted to each other
what are primary structure determined by
DNA sequence of the gene which encodes the polypeptide
why is the shape of proetin important
critical for its function
what is the primary structre
order of amino acids in a polypeptide
what causes the primary structure to twist into a secondary
hydrogen bonds
what are the 2 types of secondary structures
beta plated aheet
alpha helix
what is the tertiary structure
final 3d shape of polypeptide chain
critical for how proteins function
what are quaternary
made of 2 or more tertiary proteins joined tog
what shape is globular
spherical shape
are globular proteins soluble in water
yes
what do globular proteins have on their surface?
hydrophilic amino acids
examples of globular proteins
haemoglobin
enzymes
strenght of fibrous proteins
high tensile strenght
solubility of fibrous proteins
insoluble in water
what are on the surface of fibrous proteins
hydrophonic R groups
exaples of fibrous protiens
collagen
keratin
what type of mol is enzymes
tertiary globular proteins
defenition of an enzyme
biological catalysts that speed biochemical reactions in living organisms
4 examples of enzymes
carbohydrase
lipase
amylase
DNA helicase
what would happen without enzymes
toxins would soon build up and the supply of respiratory substrate would decrease
what is collision theory
collisions with too little energy will not produce a reaction (enzymes)
collision theory - what does rate of reaction depends on
rate of succesful collisions
is activation energy lower with or without enzyme
with enzyme
relationship between enzyme and activation energy
enzymes increase rate of reaction by lowering activation energy
what is the basis of lock and key model
shape of active sites of enzymes are exactly complementary to the shape of the substrate
whats the new version of lock and key
induced fit model
description of induced fit model
active site not exactly complementary but change shape in presence of specific substrate to become complementary
whats the name of the thing that forms in enzymes
enzyme-substrate complex
in induced fit what happens after enzyme substrate complex forms
enzyme products complex
where can enzymes act
inside the cell - intracellular
outside the cell - extracellular
what happens at 25 degrees in enzymes
- low temp , kinetic energy low
- enzyme and substrate molecules move slowly resulting in less enzyme - substrate complexes
what does an increase in temp do in enzymes
greater kinetic energy
what happens at 37 degrees in enzymes
higher temp, higher kinetic energy
-enzyme and substrate move quicker resulting in more enzyme substrate complexes
what happens at 60 degrees in enzymes
too high temp breaks hydrogen bonds in active site changing its shape
active site no longer correspondes to substrate shape
enzymes become denatured
what do small changes in ph in enzymes do
reversible changes
what do large changes in ph in enzymes do
denature an enzyme
how can enzymes be denatured
high temperatures
extreme pH change
how does extreme pH change effect enzymes
charge on active site must attract substrate mol
if theres too much H+ (acidic) or OH- ions (alkaline)
the substrate may end up with the ame charge and repel each other
enzyme concentration and substrate conc
if enzyme conc remains constant, rate of reaction will increase at the substrate concentration increases
effect of substrate conc on enzyme activty
increases rate of reaction as more substrate mols present - more succesful collisions
effect of enzyme concentration on enzyme activity
increasing enzyme concentration incrases the number of active sites available and therefore increase succesful collisions
what are the types of inhibitors
compeitive
non competitive
what does an inhibitor do
any substance which decreases the rate of enzyme catalysed reaction or stops it
what is the name of the thing when enzyme and inhibitor form togteher
enzyme inhibitor complex
what are competitive inhibitors
structurually similar to substrate mol so it can fit into the active site
what do competitive inhibitors do
prevents enzyme substrate complexes forming
where do non compeitive inhibitors bind to
anywhere else that isnt the active site
what do non compeitive inhibitors do
changes the shape of the active site so the enzyme cant fit in anymore
generally are compeitive inhibitors reversible
yes
generally are non compeitive inhibitors reversible
no
main differnece in compeitive vs non competiitve inhibitors
compeitive binds to active site
non compeitive binds to another part
effect of increasing substrate conc on compeitive inhibitor
decreases inhibitor because they both compete for active site
