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General Biology - Lesson 7-8

CELL MEMBRANE, ENZYMES
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0% found this document useful (0 votes)
8 views7 pages

General Biology - Lesson 7-8

CELL MEMBRANE, ENZYMES
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PDF, TXT or read online on Scribd
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LESSON 7: THE CELL MEMBRANE and a phosphate containing group attached

AND TRANSPORT MECHANISM to the third carbon


• Amphipathic, has hydrophilic and

PLASMA MEMBRANE hydrophobic regions

MEMBRANE PROTEINS
• Follows a FLUID MOSAIC MODEL
• Selectively permeable INTEGRAL PROTEINS
• A film only 8nm thin • Penetrate the hydrophobic core of the
• It would take around 8000 plasma plasma membrane
membranes to equal the thickness of • Many are transmembrane the
a sheet of paper completely span the plasma membrane

PERIPHERAL PROTEINS

• Not imbedded in the membrane at all


• Found on the periphery or on the sides
of the membrane

DISCOVERY OF THE PLASMA MEMBRANE

• The existence of plasma membrane was


discovered in 1890s and its chemical
components was discovered in 1915
• In 1935, Hugh Davson and James
Danielli theorize that the structures of
plasma membrane resemble a sandwich
• In 1972, Grath L. Nicolson proposed the
Fluid Mosaic Model
MEMBRANE CARBOHYDRATES
COMPONENTS OF THE PLASMA MEMBRANE
GLYCOLIPIDS
• PHOSPHOLIPID
➢ Main fabric of the membrane • Sugar chains covalently bonded to lipids
• CHOLESTEROL
GLYCOPROTEINS
➢ Cell insulation
• PROTEIN • Sugar chains covalently bonded to
➢ Transport of substances through
proteins
membrane and cell recognition
• CARBOHYDRATES
➢ Cell recognition

PHOSPHOLIPID
• Composed of 3
carbon glycerol
backbone with
two fatty acid
molecules
attached to
carbon 1 and 2,

GENERAL BIOLOGY 1
FUNCTION OF MEMBRANE PROTEINS AND ATTACHMENT TO THE CYTOSKELETON/ECM
CORBOHYDRATES
• Microfilaments or
TRANSPORT other elements of
the cytoskeleton
• A protein that spans the membrane may may have
provide a hydrophilic channel across the monovalent bind to
membrane membrane proteins,
a function that help
maintain cell shape

CLASSIFICATION OF TRANSPORT PROTEINS

UNIPORTER

• Transports substances in a unidirectional


manner depending on the concentration
gradient

ENZYMATIC ACTIVITY SYMPORTER


• A protein built into • Transports different types of molecules in
the membrane may the cell membrane at the same time
be an enzyme with its
active site exposed to ANTIPORTER
substances in the
adjacent solution • Transports different types of molecules in
the cell membrane in opposite direction at
SIGNAL TRANSDUCTION the same time

• A protein built into


the membrane may
have a binding site
with a specific
shape that fits the
shape of a chemical
messenger, such as
a hormone

CELL TO CELL RECOGNITION

• Some glycoproteins
serve as identification
tags that are
specifically recognized
be membrane proteins
of other cells CELL TRANSPORT
INTERCELLULAR JOINING MECHANISM
• Membrane proteins of
adjacent cells many • Refer to the various ways by which
hooks together in different substances can be allowed
various kinds of to enter the cell
junctions such as gap • If the exchange of substances occurs
junctions and tight
junctions
in the direction of the concentration
gradient, there is no need for energy
output from external factors

GENERAL BIOLOGY 1
• If the exchange of substances occurs
against the direction of the gradient,
inputs of extra metabolic energy are
required

1) DIFFUSION
➢ Happens when particles move from
an area of high concentration to an
area of low concentration

FACTORS THAT AFFECT DIFFUSION


• Extent of the concentration of gradient
• Mass of the molecules diffusing
• Temperature
• Solvent density
• Solubility

KEY TERMS:
SOLUTE
• Refers to the substance that needs to be
dissolved, catalyzed broken down in
order to be utilized by the cell

SOLVENT
• Refers to the substance that will 2) OSMOSIS
dissolve the solute such as water which ➢ The diffusion of free water
is the versatile solvent across a selectively permeable
membrane
CONCENTRATION GRADIENT ➢ The diffusion of solvent from an
area of lower solute
• Refers to how solute particles will move concentration to an area of
through a gas or solution from an area higher solute concentration
with a higher number of particles to one
with a lower number of particles while
being separated by a membrane

PASSIVE TRANSPORT
• Movement of a substance across a
membrane with no energy investment

GENERAL BIOLOGY 1
• ATP is hydrolyzed leading to
phosphorylation of the cytoplasmic side
OSMOSIS IN ACTION of the pump
• Phosphorylation is caused by the
TONICITY
transfer of the terminal group of ATP to
• The ability of the surrounding solution to the transport protein making ATP
cause a cell to loss or gain water become ADP

2) SECONDARY ACTIVE TRANSPORT


• Once the Na ions are liberated, the
pump binds two molecules of K to their
respective binding sites causing
dephosphorylation of the pump
• Two K ions are transported into the cell

3) VESICULAR ACTIVE TRANSPORT

3) FACILITATED TRANSPORT ENDOCYTOSIS/EXOCYTOSIS

PHAGOCYTOSIS/PINOCYTOSIS
ACTIVE TRANSPORT
• Uses energy to move solutes against
their gradients
• To pump a solute across a membrane
against its gradient requires work, the
cell must expand energy
• Uses carrier protein

RECEPTOR-MEDIATED ENDOCYTOSIS

1) PRIMARY ACTIVE TRANSPORT


• Binding of three Na ions to their active
sites on the pump which are bound to
ATP

GENERAL BIOLOGY 1
LESSON 8: STRUCTURE AND FUNCTION EXAMPLE OF ENZYMES
OF BIOLOGICAL MOLECULES - ENZYMES
• AMYLASE
ENZYMATIC BROWNING ➢ An enzyme found in saliva that
helps digest starch
➢ Peeling, bruising, or cutting fruits cause them • TRYPSIN
to release enzymes like polyphenol oxidase ➢ An enzyme found in the small
(PPO) that, with the presence of oxygen in intestine that helps break down
the surrounding air, goes into chemical proteins
reactions of plant compounds. These • LACTASE
chemical reactions produce brown pigments ➢ An enzyme that helps in breaking
through the process of enzymatic browning. down the sugar lactose
• PEPSIN
REDOX REACTIONS ➢ A stomach enzyme that serves to
digest proteins found in ingested
➢ Oxidation and reduction occurred when
food
peeling or cutting fruits resulting to an
enzymatic browning. These pairs of ENZYMES STRUCTURE
reactions are called oxidation reduction
reactions or redox reactions
➢ Oxidation-reduction (redox) reaction is a
type of chemical reaction that involves a
transfer of electrons (loss or gain) between
two species.
➢ EXAMPLE:

ENZYME
➢ Organic or biological catalysts • PRIMARY STRUCTURE
➢ Catalysts - substances that speed up a ➢ Refers to the specific sequence of
reaction without being used up, amino acids in a polypeptide chain
destroyed, or incorporated into the end ➢ Order of amino acids in the
product polypeptide chain is derived from
➢ Almost all enzymes are proteins with gene it is transcribed from
amino acid chains which lower the ➢ Different enzymes have different
series of amino acids
activation energies of chemical
• SECONDARY STRUCTURE
reactions inside the cell (or catalysis)
➢ Amino acids can interact with each
➢ There is a specifically matched enzyme other and form hydrogen bonds
for each substrate, meaning to say, a resulting in chain folding
substrate will only fit to its specific ➢ The protein chain can fold into two
enzyme ways: α helix and β pleated sheet
➢ Enzymes are reusable, meaning to say ➢ In α helix, the chain wraps around
they can be used over and over again for while in β pleated sheet, the chain
a reaction folds on top of itself
➢ Enzymes usually end with the suffix -ase • TERTIARY STRUCTURE
➢ The protein could further fold up
due to the bonds between the side
chains (R groups) of the amino acids
forming a three-dimensional
structure

GENERAL BIOLOGY 1
• QUATERNARY STRUCTURE LOCK AND KEY MODEL
➢ Aggregation of the different
polypeptide units ➢ This model asserted that the enzyme and
➢ The quaternary structure is the substrate fit together perfectly in one
overall protein structure instantaneous step

PARTS OF ENZYMES INDUCEDA FIT MODEL


• SUBSTRATE ➢ This model asserted that as the enzyme and
➢ Chemical reactants to which an substrate come together, their interaction
enzyme bind causes a mild shift in the enzyme’s structure
• ACTIVE SITE that confirms an ideal binding agreement
➢ Location within the enzyme where between the enzyme and the substrate’s
the substrate binds. transition state.
• APOENZYME
➢ Protein portion of the enzyme ENZYMES IN CHEMICAL REACTION
consisting of amino acid chains
➢ Inactive part of the enzyme which ➢ Chemical reactions involve the breaking
requires cofactor for its activity and forming of bonds in a molecule which
• COFACTOR leads to the creation of new products.
➢ A non-protein component that Certain types of chemical reactions require
assists the enzymes during catalysis higher amounts of energy for it to happen.
of reactions The initial investment of energy to start a
➢ Can either be inorganic ions or reaction is known as Activation Energy
organic compounds (free energy of activation).
• HOLOENZYME ➢ Heat can hasten the rate of reaction by
➢ Complete, functional enzyme putting the reactants to the transition state
which is catalytically active (or unstable state in a reaction) but this
➢ A cofactor and apoenzyme would not work well in biological systems.
conjugated together A high amount of heat can denature
proteins and speed up other reactions that
• COENZYME
are not essential.
➢ A non-protein organic molecule
that is loosely associated with the ➢ Enzymes are used by the cells instead of
enzyme heat to surmount the activation energy
barrier. In catalysis, enzymes work by
➢ Can be removed from the enzyme
lowering the activation energy by
and undergo reactions to combine
contorting the substrate’s molecules.
again with enzyme
FACTORS AFFECTING ENZYME ACTIVITY

ENZYME ACTIVITY
➢ Enzymatic proteins are sensitive to its
environment so its structure can change in
response to the condition it is in

➢ Optimal conditions - conditions where


enzymes work effectively and efficiently

TEMPERATURE

• The optimal temperature for enzymes is


about 37 degrees Celsius (or 98.6 degrees
ENZYMATIC-SUBSTRATE COMPLEX Fahrenheit)

➢ Formed when an enzyme binds to substrate

GENERAL BIOLOGY 1
• There are also enzymes that work well at • NONCOMPETITIVE INHIBITOR
lower and higher temperatures ➢ A molecule that binds to another
site on the enzyme and blocks the
enzyme from doing its job. Meaning
to say, the substrate can bind but
reaction is blocked.

pH
• ALLOSTERIC REGULATION
• The optimal pH range for enzymes is 6-8 ➢ Any form of regulation where the
• There are some exceptions for this such as regulatory molecule binds to an
enzymes in the digestive system enzyme someplace other than the
• Pepsin works best at very low pH while active site. The place where it binds
Trypsin works best at alkaline environment is called the allosteric site.

• FEEDBACK INHIBITION
➢ The end product of a metabolic
pathway acts on the key enzyme
regulating entry to that pathway,
REGULATORY MOLECULES keeping more of the end product
• COMPETITIVE INHIBITOR from being produced.
➢ A molecule that can bind to the
active site and simply block the
substrate from binding.

GENERAL BIOLOGY 1

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