lipids

defined by insolubility in water

store energy (fatty acids/tryglycerides)

form core structure of biological membrane

other roles (signaling, protein anchors,
cofactors, etc), involve smaller quantities
fatty acids

flexible due to ability to rotate around
carbon-carbon bonds

extended conformation most stable due to
steric constraints


oleic acid

most common fatty acid

18:1 cis-9

18 carbons, 1 cis double
bond between 9 and 10
essential fatty acids

fatty acids needed by, but not synthesized in,
the body


get from
plants

used to
synthesize
arachidonic
acid
arachidonic acid

precursor for
eicosanoids

used to make
prostaglandins (signal
compounds)

physiological effects
(ex; relaxation of
smooth muscle)
partially hydrogenated fatty acids


generated from polyunsaturated fatty acids

chemically reduced

margarine

bad for you (increased LDLs)
triglycerides/triacylglycerols

high amount of fatty acids stored in these
compounds
triglycerides/triacylglycerols

stored in adipose tissue

mono- and diacylglycerols less abundant







energy reserves

1 g fat yields 38 kJ energy

1 g protein/carb yields 17 kJ
energy
why fatty acids?

fatty acid chains can be broken down and
used for energy

two carbon fragments converted to acetyl-
CoA

generate energy through oxidative
phosphorylation
glycerophospholipids


glycerophospholipids





variety comes from various groups that are
bound to phosphoric acid


glycerophospholipids





variety comes from differing fatty acids
bound in positions 1 and 2

typically, position 1 is a saturated fatty acid,
while position 2 is an unsaturated fatty acid

less frequent fatty acid containing structures
sphingolipids
ether
glycerophospholipids waxes
steroids

hormones
monolayers, micelles, bilayers

form spontaneously

critical micelle
concentration (CMC)

eventually, bilayers will also spontaneously
form from phospholipids

to prevent exposure of hydrophobic center,
the bilayers fold in on themselves, forming
closed vesicles
fluid mosaic model of biological membrane
1972
membrane proteins


associated with the biological membrane

perform functions associated with the
membrane

receptors
transporters
channels
other functions
peripheral membrane proteins

associate by weak forces


can be separated from this
association by similar
treatments to separate
quaternary interactions

urea

carbonate (high pH)
integral membrane proteins

firmly anchored in membranes
intermembrane portions
nearly always -helix or -
sheet
single
transmembrane
segment proteins

transmembrane
spanning
segment typically
-helix

ex; glycophorin
amino acid stabilization energies







monoamine oxidase

important for
neurotransmisson

MAO inhibitors

treat psychiatric disorders
bacteriorhodopsin

7 hydrophobic, membrane spanning
domains
connected by non-
helical loops on
either side of the
membrane

outer AA residues
interact with charged
heads of
phospholipids
bacteriorhodopsin

7 hydrophobic, membrane spanning
domains
light-driven proton
pump in bacteria

related to
rhodopsin

model for
membrane proteins
hydropathy plots

based on 1 structure

analysis of amino acid sequence to
determine likely membrane spanning
sequences




glycophorin A




bacteriorhodopsin

-barrel protein

different 1 structure pattern from
transmembrane proteins with -helices

-strand alternates from one side of the barrel
to the other

-helix more economical for membrane
spanning, more prevalent in higher eukaryotes
facilitated diffusion

passive transport

can be specific for
a molecule or allow
non-specific
molecules with
particular
characteristics


facilitated diffusion

passive transport

can be specific for
a molecule or allow
non-specific
molecules of a
particular
characteristic

transporters
facilitated diffusion

ex; GLUT1

glucose transporter found in RBCs

allows for diffusion 50,000 times faster than
uncatalyzed transmembrane diffusion
three classes of transport systems

GLUT1; uniport

chloride-bicarbonate exchanger

also found in RBCs

needed for CO
2
transport from tissues to lungs

antiport

like GLUT1, believed to have 12 membrane
spanning -helices
CO
2
freely moves across
membrane

picked up in tissues,
converted to HCO
3
-
, which
goes back out into the
blood
in lungs, HCO
3
-
picked up
again, converted back to
CO
2










increases rate of HCO
3
-
transport across RBC
membrane more than a millionfold
P-type ATPases

cation transporters

reversibly phosphorylated by ATP as part of
the transport cycle

phosphorylation induces conformational
change that triggers movement of cation
across membrane
P-type ATPases
ion binding
Na
+
/K
+
pump

3 Na
+
out for 2 K
+

in

generates
electrical potential
along with
concentration
gradients
cytosol
lumen
secondary active transport

ATP synthase

part of oxidative
phosphorylation
fundamental conditions for life


1) self-replication


2) catalyze chemical reactions efficiently and
selectively

generate energy!
enzymes


allow for harnessing of energy in a controlled
way

thermodynamic potentiality
enzymatic pathways


enzymes sometimes require additional
components for functionality

cofactor

one or more inorganic ions

ex; Fe
2+
, Mg
2+
, Mn
2+
, Zn
2+


enzymes sometimes require additional
components for functionality

coenzyme
more complex organic or metalloorganic
molecules

can be derived from vitamins

ex; heme (cytochrome a
3
),
vitamin C (prolyl-4-hydrolase, collagen)
enzymes sometimes require additional
components for functionality

prosthetic group

tightly bound coenzyme
enzymes sometimes require additional
components for functionality


holoenzyme; enzyme + cofactor/coenzyme


apoenzyme; enzyme cofactor/coenzyme
enzyme classification

based on reactions they catalyze

many enzymes are named by adding ase to
substrate/activity

urease hydrolyzes urea

DNA polymerase generates DNA polymers
enzyme classification

oxidoreductases
transfer of electrons

transferases
group transfer reactions

hydrolases
hydrolysis reactions
enzyme classification

lyases
addition of groups to double bonds or
formation of double bonds by group removal

isomerases
transfer of groups within molecules to yield
isomeric forms

ligases
formation of bonds by condensation reactions,
usually coupled to cleavage of ATP
enzyme classification

ex;

ATP + D-glucose ADP + D-glucose-6-phosphate

ATP:glucose phosphotransferase

common name, hexokinase
catalysis

most reactions are slow in physiological
conditions

many reactions require formation of unstable
intermediates

enzymes provide specific environment that
allows reaction to occur more rapidly
active site









specificity
affinity
catalyst



S
P
catalyst

enzymes lower activation
energy (G

) of reactions
G unchanged by enzymes

favorability of the reaction remains the same

for this reaction, forward G
backward, +G
S
P
energy barriers

allow for stability of complex
molecules
without barriers, compounds (such as
sucrose) would break down spontaneously

enzymes lower barriers within cells to unlock
energy from compounds or generate complex
compounds
S
P
how do enzymes lower activation energy?


stabilization of transition state

side chains/cofactors/coenzymes associate
with substrate in active site

can form temporary covalent bonds

bind with weak forces
how do enzymes lower activation energy?


form enzyme-substrate (ES) complex

releases small amount of free energy that
stabilizes interaction

binding energy (G
B
)

G
B
is maximized with formation of transition
state

transition state