Professional Documents
Culture Documents
-5
5S
Bio 101
ch3
-
concept -> Chemistry of water
&
. 3
The
oxygen hydrogen is
is
cartially
I
neg ative S -
partially
Positive S I
xThe properties of water arise from attraction
between
↓ opposity
charged molecules .
The
to partial y positive hydrogen of
of one molecule is attracted
partial y negative ↓
oxygen nearly molecule
a
Held togather
by awagen bond
- When water is in its liquid form hydrogen bond are
,
vary ragile ,
to as
strong
covelant bonds
as
a a are
constantly forming
new bonds with a succession of partners
coverlant
en bonde
-
-ge en
-
-
-
Concept
32 Four
emergent properties of water contirbute to
Earth's forlife
Suitotabimoderate
lity temprature expansion
Cohesive behaviour ,
ability ,
more
Structured
I
:
liquids
togather
result of cohesion due to
as a
hydrogen bonding us high
surface tension
-
Surface of aliquid
conducting cels.
water evaporates from leaf
as a
,
hydrogen bondfurther
Cause watermolecules
leaving the
down and upward Pull is transmitted
vien to
tug on
-clinging one
counterthe
downward Pull
-
-
-
-
-
-
of gravity
are nee
·
water absorbs heat from warmer air and releases heat
to cooler air" with tempreture"
only a
slight change in its own
movment of atoms
,
volume
A heat Thermal
:
energy
transfered from one
body of matter to
another
of water by PC
kcal =
1 , 000 cal
specific heat : -
amount of Cal =
4 1845
-
,
15 =
0 .
239 cal
heat that must be absorbed
lost for lg of that substance to
change
tempretuve
or its y
of the
Because high specific heat of water , water will
4 change its tempreture less than other liquids .
heat must be
I temprature]
· moderate air tempratures stablize ocean
· resist changes in
organisms temprature
heat of vaporization->
a liquid must abork for ofthe wantine teacher
Ig
liquid to gaseous state
* Solution :
-
a
liquid that is
completly homogenous mixture of
two or more substances
* Solvent :
dissolving agent
of a soultion
is
one in is
the solvent .
↳
water is versatile solvent due to polar covelant
avery
bonds
example/Nact placed in water->
to soduim cations
,
hydrogen regions
are
positivly charged and attracted to
choloride
animus
:
as a result water molecules Surround the individual
Soduin and Choloride them andsheilding from
ions
superating them each
other
0
O
Cl 0
0 Nat 0
·
O be ionic to dissolve
0
⑳ Do
o
in water
(Polar non-ionic bonds
& a substance
water
can be hydrophilic
Cotton
without
actually dissolving
in
hydrophobicformsubstances that
·
molecule
* Mole : -
Molarity -
number of moles of solute per lifer of solution
-
-
-
-
-
-
break/stretch
difficult
surf in
it to
measure of
is
how
->
O -
~
v
0
*
0
x
⑦
-
⑦
⑰ ⑦
⑦ ⑦
polar covelant hydrogen
covalant
->
hydrosen
-> adension
-> cohesion
Macromolecules ->
large -
complex molecules
Carbohydrates , protiens and Nucliec acide
Polymer : a
long molecule consisting of similar
many
-
building blocks
units that
monomers
repeating serves as
:
IEnzymes
up chemical
are specialized macromolecules that speed
reactions
I
within
example
- our
body
dehydration synthesizing reaction
a
polymer
hydrolysisbreaking digestion
down a
Polymer
when two monomers bond when polymers are
together through the ↓2assembled to
monommer
loss of a water molecule (reverse of dehydration)
HO I 2 3 H Ho H
HO 1 -4 H
S
H0
Fizo W
↓H20
H Ho-D-R--H Ho-- H
1 2
-
-
-
3 n -
of
Diversity Polymers
·
a cell has thousands of different
Macromolecules
it varies the cells of organism , within
·
among an
a
species and even more between species
set of monomers
,
of sugars
CnHenOn n- number of Carbons
c =
0
*
hydroxyl group-OH
.
·
classifying Monosaccharides : -
1) location of
is either a ke/carbonyl group , a monosacarid
Skeleton it accurate
linear carbon is not
completly
C in aqueous soultion five and six -
Monosacharides
/ ↳
major fuel for raw material
cellular work for synthesis
of other type
of organic
molecules (fatty +
amino aecids)
disaccharide -> two monosaccarides joined
together through glycosidic linkage a
a ,
1 ,y
glycosidic
linkage
·
-
oseXse ose -
&
cose x ose e
- -
linkage
·
sexose
Lactose
3 -
joins
carb
mo
-
↓
ring even
though its a
hexoses .
lactose intolerance
-
common condition in humans
wholock
glucose
tase:theenzyme tatee
galatal
broken down
sugar is
bacteria .
by intestinal
polysaccharides polymers
-> of sugar with
/storage polysaccharides]
startchy a storag e polysaccharide
of plants consists of glucose monomers
↳
synthesizing startch enabels plants to stockpile
surplus glucose
(forPotato
cells
tubers fruits
, of wheat , corn , rice are major source of
Startch in human diet
form
-Simplest
of
Startch
->
- -4 linkages
-- -Glinkages
2
-
C
animalstorage
B
·
glycogen-> storage
a
Polysaccharide
in animals liver and muscle cells
->
↓
Breakdown of glycogen releases glucose when
demand of Sugar increases
Compenent
like startch it with 1-y
is a
polymer
with a different
glycosidic linkages but
ring structure
-
Gurgiul straighte
* Cellulose is never branched
6
some hydroxyl group hydrogen bond with the
hydroxyls of other parallel cellulose molecules
*
Enzymes that digest startch by hydrolyzing
a linkages Can't
hydrolyze /3 linkages
*
Some microbes use
enzymes to digest cellulose
x
many herbivores
from cows to termites have
symbiotictel,
with these microbes
all
Chydrophobic
·
->
So Synthesis
fat
of one
mole call
- -
requires of
-
- removal
3 water
molecules
triglyceride
triacylglycerol
.
The relativly non-polar <-H bonds the hydrocarbon in
each
fatty acid is joined to a
glycerol by a
-
denaration reaction resulting in an easter
X I linkage
tri acylglycerol
Bond between
triglyceride
a
carboxyl and hydroxy
group
*
fattydifferent
three
acids can
kinds
all be the same or of two or
Saturated
of
fatty acid
possible and
-
maximum number
double bonds
hydrogen no
unsaturated
more
fatty acids - has
double bond with one fewer
,
a one
hydrogen atom
or
on
each double-bonded carbons
I
normally a cis that creates
bond a
kink thein
hydrocarbon
-
L
saturated unsaturated
coronarydisease
heart
adipose cells
* adipose tissues also cushions vital
organs
0
*
X
I -
at O
!
dir
0 2
-
olt
0
=
OH
or
-- c
-
=
C
- c
d↑
- -
-
-
not a ll
X
-
-
·
an
-
~
0
X
X
X
0 -Kind
Similar to fat molecule but
phospholipfatty
ids
two
->
acid and a
glycerol
a
,the third
hydroxy/group
group isattatched to a ⑱hat
P
C
negat i ve
-
Typically an
polar molecule
additional
is
small
linked to
charged
a
or
phosphate group
"has
-charg e
a
->
&⑤↳hyde
e
phosphate group ↑
a
hydrophillic
water
head that has an
affinity for -p =o
↓
glycerol- C-CH2
->
I
H
H2
fan) is s
choline
I
Pr
-
&
glycero &
↳ easter
linkase
phosphatidyly choline
M
when Phospholipids added
to water
are self-assemble
double layer called bilayer
into
S
PThe hy drophillic head are outside the bilayer
D hy drophobic head points toward the interior
of bilayer
A bilayer forms a boun dary between cell and
-its external environment-----
Steroids > lipids characterized by
carbon Skeleton of four fused rings
a
living being
S
depends on protiens
they account more than So x of the dry mass of most cells
catalysts
I
.
I
each
type of protien have a unique three
dimensional shape
peptide bond a
a
polymerof amino acids ->
Polypeptide
Protien biologically functional molecule made
of each foiled
up one
into a specific
or more
polypeptides
three dimensional structure .
,
and coiled
Defensive Protiens
①
Enzymatic Protien ②
Efunction protection
Sfunction :
selective acceleration ex/
: -
against disease
antibodies
,
of Chemical reaction
ex digestive protien
④ Transport Protien
↓function :
-
transpor substance
O Sstorage protiens
3 ex hemoglobin
function sLove amino acids
..
ex/casein (milk) ,
ovalbumin
(199)
⑤ hormonal protien ⑥ receptor protien
S
Sfunction -coordination of
: an function :
Response of cell to
support
function motion ex Keratine
ex/myosin ,
activ Collagen
das tin
Amino acids
organic molecule with
an
both
- group and aC
-
an amino carboxyl group
S
at the center of an amino acide there's
carbon atom cal led
aysmetric R
carbon
IO
C- C
S N -
OH
its four parterners are
i
an amino group, a
carboxy group
atom ,
a
hydrogen a variable group (side chain)
bodde
a Polypeptide E
repeating over
of
and over the process
,
peptide bonds
R
H
-
↑ /o
-
C-
A
-I WOn C
N-termines
epeating
terminus
sequence of
atoms -> backbones
Structure
the
Polypeptide
-from Pr the
Protien Structure
C The
and
&
function -
·
specific properties of protien results from their
is
intricate three-dimensional architecture
* The term
polypeptide is not
synonymous
with the term protien
S
Thi
fol d i n g
the formation of
is driven
various
and reinforced
bonds in
by
chain , which
in turn depends on the
sequence of amino acids
↓
A protien specific structure determines
how it works
,
it depends its ability to
on
L
V
W
Space-fil
"Emphasizes
ling model Ribbon model
-
shows
I
wire-frame
the overall
only
globular shape" the
polypeptide shows polypeptide
backbone backbones with
side chains
extented from it
trans
↳
pert shape) (solid shape)
6 structural details
show the shape as
well as some internal are not needed
details
Four levels of protien structure
repeating constituents of
polypeptide backbone
within the backbone
oxygen atoms have partial
,
the
Nitrogen
attached
to
negative charges ,
and the
hydrogen atoms have partial
positive charges i therefor hydrogen bonds form
↳ these bonds weak because they are
individually are ,
delratenten
two
of
or more
segment
polypeptideside chain
laying sidebly
between
every
fourth amino acid
S
ex) A heratin
③ Tertiary structure -f overall shape of a
polypeptide
resulting from interactions between R groups of various amino
acides
V ↓
hydrogen
↳
en
transthyretin ↓
↑
3 polypeptides
C
-
↳identical
so
polypeptides
norpolyopeptide
mponent
any
With atom
ironthat binds
gen
Sickle-cell disease -> A structure
I change in
Primary
⑪ Even a slight change in primary structure can affect protiens
shape and to function
ability .
Sickle-cell disease :
inhertied blood disorder , is caused
acid
E
RBC
into
agregate
a sickle shape
what determines a
protien structure
addition to structure
in
primary
[Physical and Chemical Condition]
↓
Eempreture
X
PH
denaturation
salt concentration
loss of
-
native
: -
a protien's
structure -> in active and in functional
Protien folding in the cell
Misfolding of
polypeptides is a serious problem
7
-
madcow
cystic fibrosis Alzheimere Parkinson's disease
S I
⑯
X-Ray crystallgraphy
-Nade
A
is
diffraction of an
↓
ene
beam by the atoms X-ray
of
a
crystallized molecule
-
electr
cyromicros
om By
Col
* Bioinformatic
N -
some protiens do not
ere
genes consists of DNA which belongs to the
class of compounds called nuciec acide
made of
· Nuclic acid
-Polymers
called nucleotides
:
-
monummers
↓ -
deoxy ribonudiec acid ribonucliee
Acid
"DNA"
-
"RNA"
gene expression
from
& DNA is the
genetic material that orgnasims inherit
their Parents
& each molecule
chromosom contains one
long DNA ,
usually
several hundred
carrying more
genes
or
3
a
given gene through DNA molecule
can direct synthesizing atype of
RNA called Massenger RNA
R
unti
L croter W
mRNA
ma
interacts
I
with protein's
"Central
dog
synthesizing machenariy
to direct synthesizing polypeptide
·
The sites of Protien Synthesie
are cellular structures called Domes
↓
pin eukaryotic
but DNA resides
cell ,
ribosomes
nucleus
are in
asi
in I
↓ region between
MRNA
conveys genetic instructions nucleu and cell
for
building protiens from nucleus outer boundry
to
cytoplasm
-
nitrogenous base !
-
- - -
pyrimidine purine
Ehas one ↳
I Nin
six-membered membered
ring fused
six
of carbon and to a five membered
ring atoms
ring
nitrog en
WHz 0
11
-
-/
I Guanine
xRy/Ree,Y
N
- L
N
H e
cytosthe Adenine
110
L Y
11
L ↓
·*
/
HN C
C
1
/
·
DNA-
on the Second
deoxyribose
Carbon
m lacks an
oxygen atom
·
RNA- ribose vo
one to
The
linkage of nucleotides into
condensation
polynucleotides involves a
reaction H
distinctly
X ⑧ -
Phosphate a
hydroxy /COH)
attached to
5'carbon group attached
to 3'Carbon
⑧
structure of DNA and RNA
DNA RNA
has two
·
Strand
exsists as a
single
an
imaginary axis
forming
are helix ·
complement ary pairing ofcan
occur between regions
sugar Phosphater
·
Two two RNA molecules , or even
direction
. anti Parallel] same RNA-> allows it
to take on Praticular
· Two strands three dimensional shape
necessary for its function
heldby hydrogen
between paired G +RNA
bases
A -
↳
this feature makes it ·
RNA may have PreceededDNA
to genrate two
possible of DNA
identical copies
Cell Structure and function
Light Microsca(M) : -
visible
light pass
lenses
through
the specimen then
through glass
.
Ihrezimportant patters
-
of
microscopy : -
*
light microscopes can magnity effectively about 1 000 time the
,
low to
study organelles
-
~
C
C
=
-
a
a
~
it
1 1 -,
je -
- -
(Normarskil
Bright feild -> Differential inference contrast ->
·
light passes directly
- - =
exagrate differences
·
-
in
density
specimen Most
th ,
image
-
almost appears 3-1
---
-
.
Preserved which
e
Is them
· Phase contrast : -
Variation
-
to enhance Contrast
specimen
-
-
location of specific
- -
amoffluvoscene
Molecules are revealed
-
-
out
focuslight eliminated
-
by labeling
--
molecules with byturing sharinges at
fluroscent orantibodies , which different places , creating
-
--
sorbs avaidetation e 3-D
a much sharper
image .
--
- -
-
p laces digitally
,
-
ited
molecules
at
- and their position
re
-
light
eource -
rded,
->
,
many
-
diff
places "breaks"
-
the
- - -
resolution
- limit . The
size
-
of each dot is well
-
-
below the 200 nM
-
-
In brightfield microscopy, light passes
-
Describe the process of brightfield directly through the specimen. The image
--
That
microscopy. has little contrast and staining with dyes can
passes
-
-
light
enhance contrast.
-
uses
it can be stainc
through specimen ,
contrast
enhancing
E
uses user to
creat
planes.
-
of
-
enhance contrast in unstained cells.
implifying variation in
density
by exaggatrality density
creatine "
"
avoscene
Describe the process of digitally removing The process digitally removes out-of-focus
out-of-focus light in phase-contrast light and reassigns it to its source, creating a
u?
microscopy. much sharper 3-D image.
in
Iwrong
deconvolution
question
optical
Locations of specific molecules are revealed
How are locations of specific molecules by labeling the molecules with fluorescent
fluorescence
-
by
radiation and emit visible light.
Labeling them -
or antibodies which
absorbs
is nie light
let light and
dye ,
What are the organelles called that appear The organelles called mitochondria appear
orange in the fluorescently labeled uterine orange in the fluorescently labeled uterine
cell? cell.
-nitochondera
electrons
(EM)
Transmission electron microscopes -> aims an
electron beam
throug a
very thin section of specimen
new developed type
cryo-electron Microscopy
↳allows specimen
E
disadvantage of SEM and TEMG to be preserved
at extremly
low tempretures
the methods Customarily to Prepare the specimen killthe cells
and introduce artifacts that do not exsist in cells
living
·
Confocal and deconvolution microscopy providesharper
images of three-dimensional tissues and cells
· New
techniques forlabeling cells improve resolution .
·
super resolution allows one to
distinguish
structures as smalles 10-200m across
⑧
⑧
-
-
-
-
E
allows specimen
at low tempratures This
extremly .
specimen of tissues or
avoids the use of preservitaves , a
visualization of structures in their
l owing aqueous
protiens
solutionsof
are frozen
cellular environment at tempratures less
Mean creations
arePassed In reene
the molecule .
cell fractions
takes cell apart and sep rates
the major organells and Subcellular Structure from
one another .
at lower speed->
larger components
-
waste
↑
nuclei and cellular debris
2 -
Mitochondria and Chloroplast
The
liquid above the is
at
higher speed .
- -
Concept 7 2
:
- X I -
->-
:S
Prokaryotic .
Eukaryotic
-
: -
Bacteria Protists (unicellular
Eury
· ·
·
Archaea ·
fung ;
·
animals
·
plants
Comparing prokaryotic and
Eukaryotic cells
soup , it contain
regions
↳
carrygenes in
form of DNA
the surrounded
by protiens *
Eukaryotic
where specific reactions
tapae generally
are
much larger
Ribosomes_
makes protien
Plasma membrane
e Selective Barrier that
allows sufficient passages of oxy gen ,
nutrients and waste
to service the volume of every cell .
H
for each sequare micrometer of
membrane of
limited amount practicular
only a
I
largersmaller
organisms
than
do not
generally have
larger cells
org ansims -
↓
a
sufficiently
Area to volume is especially
high ratio of surface
important in cells that
as intestinal cells .
structers
surface of some
&
on the
Prokaryote
ventioned where
- ->
regionDNA
↳enbraue is
located
)
locomototion of
organdle Someprokaryote
Eukarytoic Cells
I
it has extensive ,
elaborately arranged internal membrane
,
H
The basic fabric of biological membranes is a double
layer of phospholipides
and other lipids .
However ! ! each
, type of membrane has a unique
Composition of lipides and suited
Protiens to that membrane's
specific function I
ex/enzymes embedded in the membrane of organelle called
Mitochondria function cellular respiration
in .
-
335 5 .
-
S W
I
E
-
S-
Y -
↓gS j"W
S
> -
.....
S -
Concept F3 .
-
* nucleus : -
houses most of cell's DNA
* Ribosomes : -
*
Nu Fryfic Stan ment reiemerch , naria
and chloroplast)
by mechanically supporting
nuclear envelope
matrix
O +
E
-~
WA is to called⑧
discrete chromosomes
·
organize --
B
aromatin the and Protiens
xo
making
:
-
Coil DNA molecule
up chromosom Protien
- ③
⑧ sociated
with
protions
①
3 organized
discrete
called
anromworme
into units
ente complex of
shromosome
protien and DNA making up
-
rRNA is
synthesized here
# protiens imported from cytoplasm are assembled with
~BNA into small and large ribosome subunits
I
The subunits exsit the nucleus through the nuclearlores to
cytoplasm , where a
large and smal subunits can beassembled
into ribosomes
Protiens -
<
2
bound Ribosomes
Free ribosomes C
(suspected in
cytosol)
attacheoutsid tie
(or nuclear envelope
a
↓ ↓
Function within into
pinsertion
cytosol ; enzymes membrane
that catalyze the first step Packaging within
of makingsugar & certain organels
(lysomes)
export from
& cell
tF4 .
endomembrane
system many of different
:
membrane
bounded organelles of eukaryotic cells
↑
I Nuclear envelope The membranes of this
1 Endoplasmic reticulum
.
-
1 golgi apparatus through physical continuity
El
lysosomes or
by the transfer by vesicels
Evacuoles
E Plasma membrane
factory
I
-
=>
y
with nuclear
continuous
envelope
Functions of Smooth ER : -
->
from scratch
①lipid synthesis & metabolism of carbohydrates
③ detoxification of
drug and Poison ↑
storage of calcair
of Smooth ER important of synthesis of lipids
↳Enzymes are
SmoothER
other cells of Smooth ER
in liver cells
help
ity cells espically
I
adding hydroxyl to drug
molecules
ce
many
the proliferation of Smooth ER
-
-2
I -
.
J's
ER membrane into
cytosol and frigger
contraction of muscle
cell
functions of Rough ER
Secrete that
Many cells protiens Produced by ribosomes attached to
are
secreted Protiens
Most are
glycoproteins
Protiens with
carbohydrates covelantly
bonded to them
* after secretory protiens are formed
ER membrane keeps them seprate
from protiens
cytosi
in
addition to secretory
in
maki n g protiens Rough ER is
↳ it
a men brane
factoryof cells
grows in
into
place by adding phosolipides and
protiens its own membranes
* As
polypeptide is destined to be membrane
*
rough also makes membrane
ER
Phospholipides ↓
where is
Rough
ER abundant ??
secretory
tissues
apparatus shipping and receiving center
Golgi
:
after
leaving ER many transport vesicels travels
golgi apparatus
,
↳ extensive
espically
for secretion
in cells specialized
&
Golgi apparatus also manufactures some macro-
molecules
↓
Polysaccarides Pectin
->
like
=>
secretory protiensprotiens secretory products
, non
· made in the
Golgi will depart from transface
and fuse with the plasma membranes, the contents
are released and the resicels membrane is incorporated
with plas ma membrane increasing its surface avea
E-- -
-
-
e n
until
recently Biologists
static structure,
viewed
golg; as a
model of
a new golgi was
given
a
dynamic structure
my According
to cisternal model
maturing ,
as they move
bysosomes :
Digestive Compartments
-
tha
of hydrolytieyes
membac -
letsee
↓
works best in acidic environment
inside
lysosome
Hydrolytic enzymes
made by Rough ER and
and
lysosomal membranes
transfered to golgi
then
are
-
imp how are protiens of inner surface of lysosomal membrane
and digestive enzymes themselves are spared from destruction?
I
Answer/ The three dimensional shape of these
protiens protect vulnerable bonds from enzymatic attack
↓
once it exists it becomes active
phagocytosis -
"
25
-
autolThogy
↓- ↓
engulfing ancells lysosomes uses
I hydrolytic enzymes to
ex/white blood cells Macrophages
ethe
cell
-> a
↓
The food vacule formed
fuses
in this
,
way then
adamaged organelle
with lysosome becomes surrounded
a double membrane
by
and lysosome fuses
with the outer membrane
of this vesicle
↓
molecules inside
-
a cell
E central vacuoles is plant cells
develops coalescence of smaller vacules , The
by
Soultion inside the central vacuole is called sap,
es
-
-
-
of
main
repository inorganic
ions such as
randd
*
Plays a
major rule in plant growth , as the
the cell to
vacuole abosbs water,
enabling
become large with minimal invesment in
cytoplasm
often between central
& The
cytosol occupies a thin
layer
vacuole andplasma membrane , so the ratio of plasma
membrane surface to cytosolic volume is sufficent
exocytosis
mitochondria and chloroplast change energy from oneform to another
↓
and otherfules
Posynthesis
Endosymboint theory
similaraties with bacteria
->
Mitochondria anachloroplast
display
->
at least one of these cells engulfedaphotosynthetic prokaryote
ancestor of
I
Theory states -
an
early Eakaryotic becoming
chloro-
Cells ,
engulfed an
oxygen using nonphotosynthesis Plast
formed a relationship
Eventually the engulfed cell with the host
becoming endosymbiont
↳ of evelation ,
over the course merged
the host cell and its endosymbiont
into a single organism
This
of Mitochondria
theory is consistentwith
many structural
features
and chloroplast
membranes .
mitochoaria chemical
energy conversion
.
↓
found nearly all
it's in
eukaryotic cells
each of the two membranes that endoses the mitochondrion is a
collection of embeded
Phospholipid bilayer with a
unique
B
protieng .
"enhancing
[The outermembrane
↓
is smooth] productivity
i
the
,
give
folded into cristae] inneumitochonde
-
I innermembrane
membrane a
The innermembrane creats two compartments large surface
area
- -
enzymes
intermembrane mitochondrial A in matrix
space -narrow Matrix -catalyse
I
:
fragment
E
form tubular network that state
a
of flux mug in skeletal muscle
is in a
dynamic
this network has been
3-6Mm in
length ,
found in leaves and other green organsof plants/algue
! stacked
thylakoids Thylakoid
&
into granum-
-
-
many enzymes
as
,
The membranes of chloroplast devide the Chloroplast
space into three compartments
↓
- stroma
-
intermembrane thylakoid
space space
* This compartmental organization enabels the chloroplast
to convert
light energy to chemical
energy A
Note
both chloroplast and
Mitochonderia are
mobile , move
along
track of cytoplasm
use
oxygen to break liver detoxify
down alcohol
fatty acids by
into smaller molecules
transfering hydrogen
that are
mitochondria
transfered to I
and used as fuel
from poisinous compounds to oxygen
The HaO2 Produced peroxisomes is Poisonous itself
by
but the organelle also contains an enzyme that converts it to
I
water I reductase]
dispose of it
J
are sequestered away from other cellular
organnels that could be damaged
5 = 51
Concept 7 6 - cytosheleton
-
- 3,31 91
↑
: ) - - S
cytoskeleton
location
dynamic , can be reassembled in a new
the
, changing shape of cell
cell
motility requires interaction o
cyto skeleton with
motorprotiens
5heletal elements works with plasma membrane
molecules to allow cells to move
along fibers outside
and inside the cell
↓
& visceles
containing neurotransmitters molecules
migrate to the tip of axons , the
long extensions of nerve
cells
minipulate plasmamembranes , bending
-
plant cells
I a ch centrosome
* in animal cells microtubuls grow out of we ↑ some
-
within the centrosome pair a
-
-
of
les
microtubules 9
locomotor appandges
Cillia or flagella
* A each motile
⑧ cilluim
-
or flagella
I =>
"to"arrangment
eN
the
9
basal
·
body of sperm enters the egg and become
entricles
&
dyneins :
Bending of cellia and Flagellum involves this
-
Motor protien
② microfilaments "actin fillament"
-
globular protien
a microfilament is twisted into a double chain of actin subunits
Is Cresent in all
Eukaryotic cells
three dimensional network formed microfilaments
*a
by
just to the inside of plasma membrane (cortical
microfilament) help support the cell's shape
I
This network gives the outer cytoplasmic layer of
a cell
[corfex] asemisolid
consistency
Bundels of microfillaments make up the core ot
Micro Villi
nutrient cells
~ in
absorbing
cause contraction of muscle cells
myosin
* in unicellular protist Amobea and some of our Whiteb,a
localized contraction and
amoeboid
by activ
myosin are brought by
Pseudopodia
-
·
Microtubles (Tublinpolymer)
· Hollow tubes
· 25 n with 15nm lumen compression
resisting
·
·
Tubulin -> tubulin tubulin
maintance of cell ⑪ cell
③
~ motility
I
chromosom
⑭
mouments in cell division , organelle mouments
·
Two intertwined strands of actin activ
monommen
·
Fam -
·
Actin tension
bearing elements
·
maintance of cell shaper, changes in cell shapes , muscle contraction
(kerating
·
Maintance of cell shape tension bearing elements, anchorage of nucleus
and certain other organelles , formation of nuclear lamina
motor
Pro tien
attatches - -
->
-
or microfilament
-
--
-
micro-tubuls
where
are initiated
↳ made up of
nontubulin
hat ↓ Sets of microtubuls
protien
connectimicrotubuls &
triplets
== C
2 .
5
flagella
unmar
spen
cell udulates
snake like
motion driving in the the axis of flagellum
direction as
age
during
slowing - fresh
-
recovers water
strone it
,
Sweeps side
stroke
40-60 C
strokes X wass
a back
- - cillia have
and forth motion directin
moves the cellin
a
- perpendicular
to axis
of cikme
an aftatchet
called
have
- motor protiens
nein
P dy
-
-
C
*
↑
Sob
C
Entire
-
C
microtubul
The outer are
de gatherby
-
-
- 0 -
central
↓
-
- nine outer
connected
-
microtubul
two
- - -
doublet of nor
-
Cilluir extend by
-
-
-
rubulin
19 to
into basal I
cellular e
reinforced by
bundels of
↳
tensions
mitmenttermediate
anchorament"
interactionof at e
myosinnt -
0
alayerof cy toplage cycles
the cell moving over
O
tracks of altir fillaments 0
motor drivestremi
Myosin with actin
by interacter -
I ↓
actinfillamen
eac myosinprojectionmy osizand
the parallel
drives
approach E
-
(nicrofibrils Addeofaccarat a a
protiens
synthesized by an
called
enzyme
cellulose
synthase
v
crimary walls of
-
cell walls
example wood consists mainly of secondarywalls
Extracellular Matrix (ECM) of Animal cells
<
-
they span
embrane and -
an
transmit signals
their cytoplasmicsidee ee between the ECM and
filmants cytoskeleton
[integ rate changes o curring]
Example/some deve loping outside th?
and inside
cells in el
specific pathways
embryo migrateorientation
along
by matching the of their microfilament
to the "grain of fiber in the extracellular
Matrix
throug direct
physical contact
↓
it that the of wall
living would isolate
seems non cell
Plasmodes mata : -
channels that connect cells
·
Because the channels are
filled with cytosol , the cells
share the same chemical
environment ,
By joining
adjacent cells , plas modesmata
unify cells into one living
continuum
·
water Protiens
, , BNAc solutes
freely
.
can pass
light junctions Desmosomes and Cap junctions in animal cells
↳ all
,
three
types are
especially common in
epithelial tissues
* Desmosomes) "anchoring
junction"
fastening cells to
gather
into
strong sheets intermediate ,
cytoplasm
* (gab Function) "communication"
provide cytoplasmic channels from heart
muscels
or erx Do ein ne breas animal embroys
·
↑
molecules may pass
↳these protiens creat pores through which
small
Chapter 8 ,
cell membrane
8 1 cellular membranes
.
are fluid mosiacs of lipides and
protien
S
Thi molecular
Contact of
arrangment
of protien
Maximizes
with water
hydrophillic regions
and extracellularfluid
a
cytosol in
while
providing hydrophobic parts with non-
aqueous soultion .
Amembrane to gather by
drophobithe
is held
e
weak interactions
e
scauses
fluidity hydrophobic core
· Most lipids and someprotiens can shift
sideways
-
Interal
or
very rarelys flip flop
The
sideway moument of phospholipas
:
-
is
Ed adjacent cells switch
·
.
Protiens are much larger than phospholipides and move more
Slowly many membrane protien are held immobile by theirattatchment
E
to
cytoskeleton orextracellular matrix
some membrane protien tend to move in a highly
fibers by
directed manner driven along cytoskeletal
,
motor protiens ~
-
- -
&
temprature decreases
Sthe membrane remains fluid to a low temprature fails A*
if its rich in phospholipides with unsaturated hydrocarbon
Es unsaturated tails cannot pack to gather
The steroid cholestrol has different effects
, on membrane fluidity
↓ ↳
37%, human body lower temp reture
high tempretures
↓
make the membrane C
prevent i n g lightpacks
less fluid
by restraining high molecular
Phospholipid weight)
es - Cholestrol can be though of as
a
"fluidity buffer"
I
S
examcleofishes that live under extreme
thrive
of
!
at tempratures
greater than 90°c inthermal hot springs
and
geysers
Their membrane have unsual membrane lipide that
prevent fluidity
excessive of membranes at such
high
* The
abilityresponse
membranes
to
change composition of cell tempratures
its temprature has
evolved in
is in
changinglive where
that
organisms tempratures vary
③
many plants
that tolerate extreme colds Such
as winter-wheat the ,
percentage of unsaturated
Phospholipid increase autmn in , that keeps
Emet
interiorof the lipid bilayer
transmembrane -
Majority are pan
the ane
interior
PThe region Consist of one ormore
Stretches of nonpolar amino acides
Typically
-
20-30
t hydrophillic parts of the Coiled into
molecules are to
exposed aqueous ↓helix
Solutions on either side of membrane Some Protiens
.
:
Peripheral Protiens :
not embedded in lipid
surface of membranes
bilayer
at all ; bound to the
loosely
often to exposed parts of integral protiens
Eraserresi
* -
C
Cytopl a smi c sidet
heldinplace by attatchment
to cytoskeleton e
forexample// in animal cells -> membrane protiens are
attached to fibers of extracellular Matrix
called integrine .
u -
1
-> bacteriorhodopsin
-
-
-
-
secondary
true e
C
↳
ne N tirminus outside C terminus
inside
*
non-heal
-
are in contant
with the aqueous solution in extracellular
and side
cytoplasmic
->
change
shape
a
hydri
protiens in a cell surface are important in the
medical feild as well ,
↳
CDn causes
dangerous
dis covery of CCR5 provided a Safer
target for developments of drugs thatmash
this protien
The Role of membrane
carbohydrates
in cell-cell
recog
nition
example/asorting ability
of cells into tissues , to
type of neighboring
② rejection of foreign cels by the cell from another
immune system
Membrane
carbohydrates
usually mort arched
chains of fewer than I5 sug ar units
,
K ↳
bondedto
covelantly
lipids
covelantly
->
glycolipides S
bonded to protiens
glycoprotions
A The carbohydrates on extracellular silve of plasm membrane can
another ·
aysmmetrical of protiens
The
arrangment , lipide ,
and
carbohydrates as membraneis being built
-&
c -
D
-
O
C -
-
-
E
-
-
. . . . . .
E -
Oc
ept
8 2 .
theabilityto
regulate transportacros
* learn
traffic
a
steady
membrane in both
of small
directions
molecules and ions movee across the plasma
regulate concentration of in
organic ions ht ,
d ,
cat , at
do not
↳ substance cross in
discriminately
The permeability of lipid
Bilayer
The Non-polar molecules , such as
hydrocarbon , con , on are
Polar molecules
, ions cannot
directly pass
I even water
,
avery small polar molecule does not
cross rapidly relative to non-polarmolecules .
a
charged atom or molecule and its surrounding of
shell water
interior of protiene
, are even less
likely to penterate the hydrophobic
Transport Protiens
I transport
specific ions and
Protien
variety
:
of polar molecules cannot
-"Channel Protient
-
-
,
move through cell membrane units own
hydrophillic channel
that certain molecules
or ions use as a tunnel
polypeptide subunit ,
· each
water
polypeptide creats a channel that
Pass
·
it allows overall entries of 3-billion water
molecule /Te second
②"Carrier protien" hold on otheir
- passangers
and its to shuttle them across the membrane
chang shape in
away
a transport protien specific for the substance it
certion substance a
translocates(oves allowing only
, a
Concept 8 3 ->
.
b ammic
-
:
example/uptake of
oxygen by
a cellular respiration
water concentration .
OSMOSiS : -
I ain
↳ depends on
parts of concentration of solutes that cannot cross
cell membrane
hypertonic
the cell
:
-
non
will
pentrating solutes
lose water shrivel and
no net movment
die
,
probably
, if a lake becomes
hypetonicand(increase level of
die
salinity
an animal might shrivel
hypotonithec -> water will enter
cell will swell
cell faster than it leaves and
and
lyse(burst)
relativy inelastic cell wall will expand so much before it exerts force back
on wall ->
called Sturgor) Pressure
I
many polar molecules are blocked by lipid bilayer ,
they
diffuse
helpof transport protiens
passively with the
- -
carrier channel
A
aquaporins -> Facilitate the massive levels of
I
diffusion of water that occurs in plant or animal
cells
of aquaporins
ex/certain Kidney cells have a high number
allowing them foredain water from urine before its excerted
Channel Protiens that transportions are called ion channels
solutes their
against gradiant
Active transport transport that moves solutes
against
their concentration gradiant
all carrier protiens rather than channel protiens
E
Active transport enabels a cell to maintain internal concentration
as in other
types of cellular work ATP
hydrolysis
:
supplies
the
energy
for most active
hydrolysis
its terminal phosphate group is transferred
to the transport Protien [can induce protients
directly
change
its shape]
Sodaim Potassium Pump -
exchanges Nat ,
At across Plasma membrane
of cels
① cytoplasmic Nat binds to soduin-pottasium pump with high affinity when
the protien has this shape
⑳
Binding of Nations Simulates-
phosphorylation by a kinase
using at
③phosphorelation leade to a change in protien' shape reducing its affintyfat ,
Navelen 3
has affinity for ki 24" bind the extracecular
sike
on
triggering release
⑰ new shape
, ,
, a
⑥24t realesed are
of Proe
⑤ loss of Phosphate group restores protien's original shape, lower affinity for let affinity
again ,
for Nat is high
cycle repeats
or carrie
How IOR Pumps Maintain membrane Potential
side of
cytoplasmic membrane is
negative in
charge relative to the extracellular
electrogenic Pump
atransport that examples
!
:
-
-
across a membrane
↳odum Pum
I
plant fungi bacteria
, ,
Cotransport : atransport Protien CCo transporter) can couple the down will diffusion
of the solute to the "uphill" transport of protiena
against its concentration gradient
↓
plant cells uses the
gradiant of H generated by its ATP-powered
Proton pumps to drive the active transport of amino acids several other
,
sugars ,
-> active
transport
dince
Fration
gradient
a Co-transporter couples the
C
return of Ht into the cell
to transport of sucrose into the ceee its concentration gradient
against
TheH protien uses the transport Protien as an avenue to diffuse down
E Plants
its electrochemical gradianet , which is maintained by proton pump
in
Eq
↓
⑧
Natylucosefindtransporters has
co
E that reabsorption
in the
body and Sodanim levels fall
is not possible
precipitously
treat this life condition ins
To threathing
Concept 85 Bulk transport across the plasma membrane occurs by exacytoic
.
and
Endocytosis
A
large molecules , protiens and polysaccharit
such as
but instead
"packaged vesicles in
I
cels
-
Endocytosis
6 The cells asin molecules and
-
pic
rate matter
by forming
new vesicles from Plasma membrane
A
although protiens involved are different endrcytosis looks like the reverself exocytosis
,
Pocket
② as the Pocket deepens it pinches in forming
, a veside
fuses with
lysosome containing in this
way
the cell
solutes taken
by
pinocytosis are
many
in cases, plasma membranes < non specific for
that form vesicles are lined on their
cytoplasmic the substance it
Side by a
fuzzy layerof coated protiens called pits
transport
S resulting pits
s.
everthough theyundeinter
specific solutes binds to receptors ,
& C -