OCR AS Biology Enzymes & Temperature 2.1.21

Based off of spread 2.1.21 in the OCR AS Biology Text book. Notes from there!

HideShow resource information
Preview of OCR AS Biology Enzymes & Temperature 2.1.21

First 524 words of the document:

Emily Summers
Wednesday 24th March 2010
Enzymes and Temperature
Denaturation Changes only the tertiary structure of an enzyme so it can't function and
its function can't be restored, which changes the active site of the enzyme.
Mo l
ec ules/
i
o ns
i
n
a gas/
li
quid
conti
n uall
y move ar
ound ,
t
hey have
kinetic energy t
o move r
a ndomly
and
conti
n uously,
causi
ng col
l
isi
ons.
E nzymes can
catal
ase
a
react
i
o n
if
the
subst
rat
e molecul
e/s
col
li
des wi
th
t
he
act
i
ve
si
te
of
the
enzy
me
so
that
an enzymesubstrate complex i
s f
ormed.
I
f
thekinetic energy
of
the enz yme
a nd the
substr
ate
molecule
is
i
ncreased
wit
h an
incr
eased
t
emp er
a t
ure then
ther
e wil
l
b e
mo r
e collisions bet
ween enzyme and
substr
ate
molecul
es,
l
eading
to
a n i
ncreasedrate of reaction
a nd
a bi
gger
yi
eld
of
product
.
Heat & Vibration Bonds Break, Denaturation
Wh en you
a ppl
y heat
to molecules,
t
hey mo ve
fast
er
in
a
li
quid
or
g as
and t
hey
also
vibr
ate.
The
vi
brati
on s
str
ain t
he bond s
holdi
ng t
h e
mo l
ecules.
In
lar
g e
mo l
e cul
es l
ike
en z
yme s the
vibr
a t
i
o n
of
mo l
ecules c
a n
break weaker
bonds
l
ike
hydrogen or ionic bonds.
The
wea ker
bonds are
there i
n abundance
in
an enzyme
mo l
ecule and
hol
d t
he t
ert
iar
y
str
ucture
in
p l
ace,
so they
ma int
ain t
he act
ive
sit
e's
corr
e ct
,specific
shape.
Increasing temperature = Increasing bonds broken

Other pages in this set

Page 2

Preview of page 2

Here's a taster:

Emily Summers
A nd the
tert
i
a r
y st
ruct
ure i
s h eld
less
i
n
the
sh ape
o f
t
h e act
ive
sit
e needed
for
i
t
to
w or
k .
S o r
a t
e of
react
ion
w i
l
l
d ecr
e ase
if
t
he
substr
a t
e c an'
t f
it
in
the act
i
ve
si
te.…read more

Comments

No comments have yet been made

Similar Biology resources:

See all Biology resources »See all resources »