solid

water
Low
density
Tempt kinetic
at
↓
state
energy
-

-
Not strong enough to overcome
hydrogen bond
- Fixed position ,
forms rigid hexagonal lattice structure
-

Space becomes farther apart , density ↓

Structure
Properties
thermal
eg :
insulating layer
surface tension
-

24 18
High
,
~ , cohesive force ↑
-

Hydrogen ,
surface tension ↑

bond 8t8-
Hydrogen H20 molecules pulled inwards towards each other
-

-
are
,

eg: capillary
animals
-
104 50
action in
xylem/habitats for
.

Max 4 hydrogen bonds

High Specific heat capacity Low

vicosity
-

Hydrogen bond
constantly broken
Hydrogen bond constantly broken Universal Solvent
-

& reformed
X reformed Dipolar , hydrogen bond
Slide each other
easily
-

-
over
needed to increase pass through
narrow vessels
-
Forms spheres of
hydration
energy
-

more
-

with less friction good solvent for bbod plasma

eg
:

hinetic of
128
energy
Thermal buffer eg
: Blood
capillaries
eg
:

small change in
temperature

Buffers

Definitions pHd (acidosis]

-
substances that minimize the change in
pH (alkalosis) -

Kidney releases Nation

HO3 + He
+
level of solution HeLO H +H H2003
pH a >
- >
-
- -

-
most common buffer in blood is HeCOs -
> Narcos
H205 + Nat - -

H2CO3 >
- CO2 + Hoe
eliminated
-

kidney by +
-
exhaled
+
-
H+ d , pHa ,
donates H -
H ↑ , pHd ,
receives It
 Enzyme
S

action
hypothesis
S

Lock &
key hypothesis (Emil Fisher
-
active site is
rigid
the substrate
active site
exactly complements
-

Induced fit -

hypothesis (Daniel Kahsland)

-

active site is flexible

-
active site not exactly complements the substrate

Definition Characteristics
Enzymes
Biological catalyst which can increase the rate
Enzyme reactions are
reversible
mostly
- -

of reaction by lowering the activation

energy
-
Have
highly specific active site

Most of the Have

enzymes
are
globular proteins # turnover number the number of substrate
high turnover number
- -

↳ to allow
enzymes
to have that can be turned into products by elyme -
Does not
undergo chemical
changes after
3D Structure to form in unit
Site
an active one time reaction (reuseable)

Cofactors
Factors
affecting enzymatic rate of reaction

site
coenzyme
: active
temporarily
-

allosteric
concentration
Enzyme -

enzyme
activators :

any site ,
temporarily
At low concentration there's for active site
enzyme great competition rate of reaction allosteric
-

, a is
prosthetic group any site
,

permanent
- :
&
low
,

As
enzyme
concentration increase active sites available to combine with substrate
,
-

, more are

rate of reaction increases

7
Further increase in concentration
beyond certain point has effect rate of
-

enzyme
on
Inhibitors
a no

reaction as the there are no more substrate available to bind to active site substrate
,

inhibitors
concentration becomes the
limiting factor ~
Competitive
Binds to active site
M
-

bosely temporarily
,

Substrate concentration -
similar structure to substrate
At low substrate concentration rate of reaction is low
active site of
enzymes
not
occupied
-

are
Umax
,
km ↑
,
-
same
-
As substrate concentration increases ,
more & more substrate is available to bind with the ,

enzyme reversible
by adding more substrate
-

substract beyond longer increase

reaches Umax at substrate concentration
higher
-

Further increase in concentration of a certain

point will no -

the rate of reaction all active becomes the

enyone concentration
as sites are saturated ,

limiting factor
inhibitor
~
Non-competitive
allosteric site
Temperature
Binds to
permanently/temporarily
-

M
At the No structural similarities I
optimum temperature rate of reaction is at maximum
-

the
-
,
shape of
temperature will rate of reaction to change
Below
temperature
a
optimum an increase in causes
-

,
Umax ↓ km active site

1
same
-

due to increase in kinetic of molecules &

,

frequency
I

increase average energy increase in

of effective collision -

most of the time is irreversible

shut down active site
Above
optimum temperature continuous increase in
temperature will rate of reaction
Enzymes are
shape of
-

, cause
-
,

&
to
drop drastically as
enzymes are denatured
changes
Adding more substrates will not reverse the
-

pH level
-

At optimum pH level ,
the rate of reaction is at maximum effect
-

Any deviation in
pl level will cause the rate of reaction to drop drastically M

&
It is caused by disruption in ionic
hydrogen bonds between amino acid side

M
-

for its substrate

chains of active site which leads to denaturation
# km =

affinity of an
enzyme
for all available
↳ amount of substrate required
due to :
active site of substrate to be saturated
# Active site of
enzymes are
extremely specific T
- 3D Structure

side chains of amino acids

↓ & + 5 =
M
of bond that be formed
types
can

# Apoenzyme +
coenzyme =
hoboenzyme
Cron-active pistein) (non-protein) (activatedenzyme