Download senatus, miriam

The Holy Review
Miriam Senatus
a.
EXPLAIN WHY YOU ARE ALREADY A SCIENTIST
I am a scientist because everything around me has to do with science and I am
constantly engaged in science. For example when I wash my clothes or ride a bike. I
think that all of us have one time or another have asked ourselves why is the ocean
blue. By just being able to ask, that question makes me a scientist.
b.
DESCRIBE CAREER GOAL
My career goal is to attend Brigham Young University and get a degree in Education.
c.
PERSONAL VIEW TOWARDS EDUCATION
I believe that education is everything. It makes us who we are today. It molds our
mind and it is one think that will never stop. The power of learning is the best tool
mankind has been given.
d. DESCRIBE WHAT KEEPS YOU MOTIVATED IN LIFE
What keeps me motivated is the fear of failure and not living up to expectations.
Chapter 1
1.Briefly describe unifying themes that pervade the science of biology.
-Cells are an organism’s basic units of structure and function
-The continuity of life is based on DNA
-Structure and function are correlated at all levels of biological organization
-Organisms are open systems that interact continuously with their environments
-Regulatory mechanisms ensure a dynamic balance in living systems
-Diversity and unity are the dual faces of life on Earth
-Evolution is the core theme of biology
-Testable hypotheses are the hallmarks of the scientific process
2.Diagram the hierarchy of structural levels in biology.
Figure 0110
3.Explain how the properties of life emerge from complex organization.
Because the properties of life is so complicated it is very for scientist to understand
biological process. However they emerge by the interactions between components.
4.Describe seven emergent properties associated with life.
1.Order-All characteristics of life emerge from an organism's complex organization.
2.Reproduction-Organisms reproduce their own kind.
3.Growth and Development-DNA directs the path to make an organism with
characteristics of its species.
4. Energy Utilization-Organisms take in energy so that it can do many types of work
5. Response to the environment-An organism will respond to its environment stimulus
6.Homeostasis-Regulating mechanism maintain an organism internal environment even
when the external environment fluctuates.
7.Evolutionary adaptation-Life evolves as the result of the interaction between
organisms and their environment.
5.Explain how technological breakthroughs contributed to the formulation of the
cell theory and our current knowledge of the cell.
The invention of the electron microscope has revealedthe complex structure of cells.
6.Distinguish between prokaryotic and eukaryotic cells.
I know this
7. Explain, in their own words, what is meant by "form fits function."
I know this
8. List the five kingdoms of life and distinguish among them.
1. Monera-prokaryotes
2. Protista-unicellular/multi eukaryotes
3. Plantae- multicellular eukaryotes that carry out photosynthesis
4. Fungi-Organism that absorb nutrients after decomposing organic waste
5. Animalia- multicellular eukaryotes that eat other organisms
9.Outline the scientific method.
I know this
10. Distinguish between inductive and deductive reasoning.
Inductive reasoning-proceeding from particular facts to a general conclusion
Deductive reasoning-Involving inferences from general principles
11.Explain how science and technology are interdependent.
I know this
Chapter 2
1.Define element and compound.
I know this
2.State four elements essential to life that make up 96% of living matter.
I know this
3.Describe the structure of an atom.
I know this
4.Define and distinguish among atomic number, mass number, atomic weight, and
valence.
Atomic #- Number of protons
Mass #- sum of protons plus neutrons
Atomic weight-the total atomic mass, or mass number
Valence- the outermost shell of electrons
5.Given the atomic number and mass number of an atom, determine the number of
neutrons.
I know this
6.Explain the octet rule and predict how many bonds an atom might form.
Octet rule- 2 electrons can fill the first energy level and 8 electrons can fit the second
energy level and the third and other levels also.
7.Define electronegativity and explain how it influences the formation of chemical bonds.
Electronegativity-The tendency for an atom to pull electrons toward itself. Influences the
formation of chemical bonds because all elements need to be complete….so therefore
there is a need to form chemical bonds in order to be complete. Therefore
electronegativity causes bonds to occur because the of the lack of electrons that other
atoms may or may not have.
8.Distinguish among nonpolar covalent, polar covalent and ionic bonds.
I know this
9.Describe the formation of a hydrogen bond and explain how it differs from a covalent
or ionic bond.
I know this
1. Science as a Process- The chemical composition of the earth reflects the history of the
solar sysytem.
2. Energy Transfer-Atoms combine by chemical bonding to form molecules
3. Continuity and Change-Chemical reactions change the composition of matter
4. Relationship of Structure to Function-atomic structure determines the behavior of an
element.
5. Regulation-Life requires 25 chemical elements
Chapter 3
1.Describe how water contributes to the fitness of the environment to support life.
Organisms depend on the cohesion of water molecules. Hydrogen bonding makes water
molecules stick together and this cohesion helps pull water upward in themicrospic
vessels. Water has a high Ph so heat is absorbed when H + bonds break and is released
when h+ bonds form, minimizing temp. fluctuations to within limits that permit life.
2.Describe the structure and geometry of a water molecule, and explain what properties
emerges as a result of this structure.
http://occawlonline.pearsoned.com/bookbind/pubbooks/campbell_awl/chapter3/medialib/0301.jpg
It causes water to have surface tension and cohesion because of the structure of it.
3.Explain the relationship between the polar nature of water and its ability to form
hydrogen bonds.
Polar molecule Is a molecule with opposite charges on opposite sides. So therefore the
relationship there is that Hydrogen bond is a type of weak chemical bond formed when
the slightly positive hydrogen atom of a polar covalent bond in one molecule is attracted
to the slightly negative atom of a polar covalent bond in another molecule.
4.List five characteristics of water that are emergent properties resulting from hydrogen
bonding.
1. Cohesion
2. Surface Tension
3. Adhesion
4. Expands when freezes
5. Disassociation of water
5.Describe the biological significance of the cohesiveness of water.
Contributes to transport of water against gravity in plants
Water clings to walls of vessels in xylem. Helps counter downward pull of gravity.
Surface tension, Measure of how difficult it is to stretch or break surface of liquid, water
has greater surface tension than most other liquids
6.Distinguish between heat and temperature.
Heat- The total amount of kinetic energy due to molecular motion in a body of matter.
Heat is energy in its most random form.
Temperature- A measure of the intensity of heat in degrees, reflecting the average kinetic
energy of the molecules.
7.Explain how water's high specific heat, high heat of vaporization and expansion upon
freezing affect both aquatic and terrestrial ecosystems.
With high specific heat water can absorb large amounts of heat without large changes in
temperature, Large bodies of water help moderate temperature on earth
Without large changes in temperature, gradual cooling of large body of water warms air
Makes ocean temperatures quite stable .Since water covers most of the Earth, temperature
fluctuations are within limits that permit life 3. Water has a high heat of vaporization
,Keeps water in liquid state. Helps moderate Earth’s climate. Water vapor condenses to
form rain
Evaporative cooling , Helps prevent overheating . Contributes to stability of temperature
in lakes and ponds 4. Water expands when it Deeper water insulated by floating ice
Allows like to exist under frozen surface Helps make seasonal changes less abrupt . As
water freezes, Heat released to air, causes air to warm, decreasing effects of decrease in
temperature
8.Explain how the polarity of the water molecule makes it a versatile solvent.
Polar compounds -- Charged region of polar water molecules have affinity for oppositely
charged regions of other polar molecules . Molecules with affinity for water, Hydrophilic
substances (a) Hydro = water (b) –philic = loving
9.Write the equation for the dissociation of water, and explain what is actually
Transferred from one molecule to another.
Equation
a) H2O + H2O ßà H3O+ + OH— b) H3O+ = hydronium ion
b) c) OH— = hydroxide ion
c) H2O ßà H+ + OH— 2.
What’s happening a) Occasionally hydrogen atoms shared between 2 water molecules in
hydrogen bond shift position b) Electron left behind c) Results in: (1) One water
molecule with extra hydrogen (H3O+) (2) One water molecule minus hydrogen (OH—)
d) Reaction is reversible e) Most of water not ionized
10.Explain the basis for the pH scale.
I know this
11.Explain how acids and bases directly or indirectly affect the hydrogen ion
concentration of a solution.
Chapter 5
1. List the four major classes of biomolecules.
2.Explain how organic polymers contribute to biological diversity.
3.Describe how covalent linkages are formed and broken in organic polymers.
4.Describe the distinguishing characteristics of carbohydrates, and explain how they are
classified.
5.List four characteristics of a sugar.
6.Identify a glycosidic linkage and describe how it is formed.
7.Describe the important biological functions of polysaccharides.
8.Distinguish between the glycosidic linkages found in starch and cellulose, and explain why the
difference is biologically important.
9.Explain what distinguishes lipids from other major classes of macromolecules.
10.Describe the unique properties, building block molecules and biological importance of the
three important groups of lipids: fats, phospholipids and steroids.
11.Identify an ester linkage and describe how it is formed.
12.Distinguish between a saturated and unsaturated fat
13.Describe the characteristics that distinguish proteins from the other major classes of
macromolecules, and explain the biologically important functions of this group.
14. List and recognize four major components of an amino acid
15.Identify a peptide bond and explain how it is formed.
16.Explain what determines protein conformation
17.Define primary structure
18.Describe the two types of secondary protein structure
19.Explain how weak interactions and disulfide bridges contribute to tertiary protein
structure.
20.Describe quaternary protein structure.
21.Define denaturation and explain how proteins may be denatured.
Describe the characteristics that distinguish nucleic acids from the other major groups
of macromolecules.
Chapter 1
1.Briefly describe unifying themes that pervade the science of biology.
-Cells are an organism’s basic units of structure and function
-The continuity of life is based on DNA
-Structure and function are correlated at all levels of biological organization
-Organisms are open systems that interact continuously with their environments
-Regulatory mechanisms ensure a dynamic balance in living systems
-Diversity and unity are the dual faces of life on Earth
-Evolution is the core theme of biology
-Testable hypotheses are the hallmarks of the scientific process
2.Diagram the hierarchy of structural levels in biology.
Figure 0110
3.Explain how the properties of life emerge from complex organization.
Because the properties of life is so complicated it is very for scientist to understand
biological process. However they emerge by the interactions between components.
4.Describe seven emergent properties associated with life.
1.Order-All characteristics of life emerge from an organism's complex organization.
2.Reproduction-Organisms reproduce their own kind.
3.Growth and Development-DNA directs the path to make an organism with
characteristics of its species.
4. Energy Utilization-Organisms take in energy so that it can do many types of work
5. Response to the environment-An organism will respond to its environment stimulus
6.Homeostasis-Regulating mechanism maintain an organism internal environment even
when the external environment fluctuates.
7.Evolutionary adaptation-Life evolves as the result of the interaction between
organisms and their environment.
5.Explain how technological breakthroughs contributed to the formulation of the
cell theory and our current knowledge of the cell.
The invention of the electron microscope has revealedthe complex structure of cells.
6.Distinguish between prokaryotic and eukaryotic cells.
I know this
7. Explain, in their own words, what is meant by "form fits function."
I know this
8. List the five kingdoms of life and distinguish among them.
6. Monera-prokaryotes
7. Protista-unicellular/multi eukaryotes
8. Plantae- multicellular eukaryotes that carry out photosynthesis
9. Fungi-Organism that absorb nutrients after decomposing organic waste
10. Animalia- multicellular eukaryotes that eat other organisms
9.Outline the scientific method.
I know this
10. Distinguish between inductive and deductive reasoning.
Inductive reasoning-proceeding from particular facts to a general conclusion
Deductive reasoning-Involving inferences from general principles
11.Explain how science and technology are interdependent.
I know this
Chapter 2
1.Define element and compound.
I know this
2.State four elements essential to life that make up 96% of living matter.
I know this
3.Describe the structure of an atom.
I know this
4.Define and distinguish among atomic number, mass number, atomic weight, and
valence.
Atomic #- Number of protons
Mass #- sum of protons plus neutrons
Atomic weight-the total atomic mass, or mass number
Valence- the outermost shell of electrons
5.Given the atomic number and mass number of an atom, determine the number of
neutrons.
I know this
6.Explain the octet rule and predict how many bonds an atom might form.
Octet rule- 2 electrons can fill the first energy level and 8 electrons can fit the second
energy level and the third and other levels also.
7.Define electronegativity and explain how it influences the formation of chemical bonds.
Electronegativity-The tendency for an atom to pull electrons toward itself. Influences the
formation of chemical bonds because all elements need to be complete….so therefore
there is a need to form chemical bonds in order to be complete. Therefore
electronegativity causes bonds to occur because the of the lack of electrons that other
atoms may or may not have.
8.Distinguish among nonpolar covalent, polar covalent and ionic bonds.
I know this
9.Describe the formation of a hydrogen bond and explain how it differs from a covalent
or ionic bond.
I know this
1. Science as a Process- The chemical composition of the earth reflects the history of the
solar sysytem.
2. Energy Transfer-Atoms combine by chemical bonding to form molecules
3. Continuity and Change-Chemical reactions change the composition of matter
4. Relationship of Structure to Function-atomic structure determines the behavior of an
element.
5. Regulation-Life requires 25 chemical elements
Chapter 4
1.Explain how carbon’s electron configuration determines the kinds and number of bonds
carbon will form.
Because carbon usually has an atomic number of 6; therefore, it has 4 valence
electrons. It usually completes its outer energy shell by sharing valence electrons in four
covalent bonds.mergent properties, such as the kinds and number of bonds carbon will
form which is determined by their tetravalent electron configuration.
2.Describe how carbon skeletons may vary, and explain how this variation contributes to
the diversity and complexity of organic molecules.
Carbon skeletons may vary in that they may be straight, branched, or arranged in
colsed rings. Some carbon skeletons have double bonds, which vary in number and
location. Such variation in carbon skeletons is one important source of the molecular
complexity and diversity.
3.Recognize the major functional groups, and describe the chemical properties of organic
molecules in which they occur.
1. The hydroxyl group
Hydroxyl group = A functional group that consists of a hydrogen atom bonded to
an oxygen atom, which in turn is bonded to carbon (-OH).
· Is a polar group; the bond between the oxygen and hydrogen is a polar
covalent bond.
· Makes the molecule to which it is attached water soluble. Polar water
molecules are attracted to the polar hydroxyl group which can form
hydrogen bonds.
· Organic compounds with hydroxyl groups are called alcohols.
2. The carbonyl group
Carbonyl group = Functional group that consists of a carbon atom double-bonded
to oxygen (-CO).
• Is a polar group. The oxygen can be involved in hydrogen bonding, and
molecules with his functional group are water soluble.
• Is a functional group found in sugars.
If the carbonyl is at the end off the carbon skeleton, the compound is an
aldehyde.
OH OH O
| | //
H-C ¾ C ¾ C
|||
HHH
Glyceraldehyde
• If the carbonyl is at the end of the carbon skeleton, the compound is a
ketone.
HOH
| êê |
H-C ¾ C ¾ C-H
||
HH
Acetone
3. The carboxyl group
Carboxyl group = Functional group that consists of a carbon atom which is both
double-bonded to an oxygen and single-bonded to the oxygen of a hydroxyl group
(-COOH).
• Is a polar group and water soluble. The covalent bond between oxygen and
hydrogen is so polar, that the hydrogen reversibly dissociates as H+
This polarity results from the combined effect of the two electronegative
oxygen atoms bonded to the same carbon.
HOHO
| // | //
H-C-C H-C-C + H
+
|\|\
H OH H O
-Acetic
Acetate Hydrogen
acid ion ion
• Since it donates protons, this group has acidic properties. Compounds with
this functional group are called carboxylic acids.
4. The amino group
Amino group = Functional group that consists of a nitrogen atom bonded to two
hydrogens and to the carbon skeleton (-NH2 ).
• Is a polar group and soluble in water.
• Acts as a weak base. The unshared pair of electrons on the nitrogen can
accept a proton, giving the amino group a +1 charge.
HH
//
R-N + H
+
R+
N-H
\\
HH
Amine Ammonium
ion
• Organic compounds with this function group are called amines.
5. The Sulfhydryl group
Sulfhydryl group = Functional group which consists of an atom of sulfur bonded to an
atom of hydrogen (-SH).
• Help stabilize the structure of proteins. (Disulfide bridges will be discussed
with tertiary structure of proteins in Chapter 5, Structure and Function of
Macromolecules.)
• Organic compounds with this functional group are called thiols.
6. The phosphate group
Phosphate group = Functional group which is the dissociated form of phosphoric
acid (H3 PO4 ).
• Loss of two protons by dissociation leaves the phosphate group with a
negative charge.
OO
½½ ½½
R-O-P-OH R-O-P-O
+ 2H
+
||
OH O
-•
Has acid properties since it loses protons.
• Polar group and soluble in water.
• Organic phosphates are important in cellular energy storage and transfer.
(ATP is discussed with energy for cellular work in Chapter 6: Introduction
to Metabolism.)
Chapter 5
1.List the four major classes of biomolecules.
A. Carbohydrates
B. Monosaccharides
C. Disaccharides
D. Polysaccharides
2.Explain how organic polymers contribute to biological diversity.
All macromolecules are constructed from only 40 to 50 common monomers and some
others that occur rarely. The polymer has variation in the linear sequence in which the
sub units are strung together.
3.Describe how covalent linkages are formed and broken in organic polymers.
Monomers which are sub units of polymers are connected by condensation reactions,
also called dehydration reactions, The net effect is the removal of a water molecule . The
reverse of this process, hydrolysis, breaks bonds between monomers by adding water
molecules.
4.Describe the distinguishing characteristics of carbohydrates, and explain how they are
classified.
Characteristics of carbohydrates are that they include sugars and their polymers.
Organism use carbohydrates for fuel and building material.
1.Classified according to number of simple sugars
a) Monosaccharides = 1 simple sugar
b) Disaccharides 2 simple sugars
c) Polysaccharides = many simple sugars
5.List four characteristics of a sugar.
1. –OH group attached to each carbon except 1
2. Carbon without –OH group doubled bonded to oxygen
3. Aldehydes
4. Carbon skeleton
6. Identify a glycosidic linkage and describe how it is formed.
Covalent bond between two monosaccharides, produced by condensation reaction
7. Describe the important biological functions of polysaccharides.
Its important to biological functions because it serves as a storage material,
hydrolyzed as needed to provide sugar for cells. Other polysaccharides are building
material for structures protecting the cell or the whole organism. Starch also serves as a
Storage of polysaccharide in plants. Animals store a polysaccharide called glycogen.
8.Distinguish between the glycosidic linkages found in starch and cellulose, and explain
why the difference is biologically important.
9. Explain what distinguishes lipids from other major classes of macromolecules.
1. Not soluble in water
2. Soluble in nonpolar solvents
3. Mostly hydrocarbon regions with nonpolar bonds
4. Some have polar bonds associated with oxygen
10.Describe the unique properties, building block molecules and biological importance of
the three important groups of lipids: fats, phospholipids and steroids
Fats - Building blocks of Glycerol which is a 3-carbon alcohol. Fats have Fatty acids
Characteristics
(1) Insoluble in water
(2) Source of variation is fatty acid composition
Importance's
1) Energy source
(2) More compact fuel than carbohydrates
(a) 1 gram fat = 9 calories
(b) 1 gram carbohydrate = 4 calories
(3) Cushions vital organs
(4) Insulates against heat loss
Phospholipids- is a Building block of Glycerol, which has 2 fatty acids. Phospholipids is
part of the Phosphate group Properties is that the Head is Hydrophilic. The Tail is
Hydrophobic. It will spontaneously form bilayer when mixed with water
Importance's:
Major component of cell membranes
Steroids:
The Building block is Four fused carbon rings, three are 6-sided, and One is 5-sided.
Attached functional groups vary. Cholesterol is a Precursor of many other steroids such
as Sex hormones and Bile salts. It is also a Common component of animal cell
membranes, which Contributes to arteriosclerosis.
11. Identify an ester linkage and describe how it is formed.
Ester linkage is the Dehydration synthesis of water molecule removed to form bond
between glycerol and fatty acid.
(1) H from –OH group on glycerol
(2)–OH from carboxyl group on fatty acid
12.Distinguish between a saturated and unsaturated fat
Saturated
No double bonds between carbons. Hydrocarbon chain is straight, Straight hydrocarbon
chain allows for tight packing of molecules. Saturated fat is Usually solid at room
temperature. Mostly in animal fats
Unsaturated
One or more double bonds between carbons. Hydrocarbon chain bent, Bent hydrocarbon
chain prevents tight packing of molecules Unsaturated is Usually liquid at room
temperature. Mostly in plant fats
13. Describe the characteristics that distinguish proteins from the other major classes of
Macromolecules, and explain the biologically important functions of this group.
Characteristics of proteins are that they are Polymers of amino acids, Vary in structure,
Each has unique 3-D shape and 20 different amino acids.
Importance's
1. a) Major component of cell parts
2. b) Provide structural support
3. c) Storage of amino acids
4. d) Receptor proteins – involved in cellular response to chemical stimuli
5. e) Contractile proteins – movement
6. f) Antibodies – defense against foreign substances
7. g) Enzymes – catalysts
14.List and recognize four major components of an amino acid
Four major components
1. a) –COOH group
2. b) –NH2 group
3. c) R (side chain)
4. d) H
15.Identify a peptide bond and explain how it is formed.
The covalent bond between two amino acid units, formed by, condensation synthesis
16.Explain what determines protein conformation
I know
17.Define primary structure
The unique sequence of amino acids
18.Describe the two types of secondary protein structure
1. alpha helix A spiral shape constituting one form of the secondary structure of
proteins, arising from a specific hydrogen-bonding structure.
2. pleated sheet One form of the secondary structure of proteins in which the polypeptide
chain folds back and forth, or where two regions of the chain lie parallel to each other and
are held together by hydrogen bonds.
19.Explain how weak interactions and disulfide bridges contribute to tertiary protein
structure.
20.Describe quaternary protein structure.
quaternary structure The particular shape of a complex, aggregate protein, defined by
the characteristic three-dimensional arrangement of its constituent subunits, each a
polypeptide. Figure 0523
21.Define denaturation and explain how proteins may be denatured.
denaturation A process in which a protein unravels and loses its native conformation,
thereby becoming biologically inactive. Denaturation occurs under extreme conditions of
pH, salt concentration, and temperature. Proteins may be denatued if they are transferred
from an aqueous solution to an organic solvent.
22.Describe the characteristics that distinguish nucleic acids from the other major groups.
nucleic acid -A biological molecule (such as RNA or DNA) that allows organisms to
reproduce; polymers composed of monomers called nucleotides joined by covalent bonds
(phosphodiester linkages) between the phosphate of one nucleotide and the sugar of the
next nucleotide.Nucleic acids store and transmit hereditary information unlike other
groups.
Chapter 6
1. Explain the role of catabolic and anabolic pathways in the energy exchanges of
cellular metabolism.
I know
2. Distinguish between kinetic and potential energy.
I know
4. Explain, in their own words, the First and Second Laws of Thermodynamics.
1st Law- Energy can be tansformed, but it can be neither created nor destroyed.
2nd Law- Every energy transfer or transformation increase the entropy of the universe.
13. Describe the function of ATP in the cell.
An adenine-containing nucleoside triphosphate that releases free energy when its
phosphate bonds are hydrolyzed. This energy is used to drive endergonic reactions in
cells.
14. List the three components of ATP and identify the major class of
macromolecules of which it belongs.
1. Adenine
2. Ribose
3. Phosphate
15. Explain how ATP performs cellular work.
I know
19. Explain the relationship between enzyme structure and enzyme specificity.
I know
20. Explain the induced fit model of enzyme function and describe the catalytic
cycle of an enzyme. the induced fit model shows the change in shape of the active site of
an enzyme so that it binds more snugly to the substrate, induced by entry of the substrate.
. Substrate binds to active site a) Enzyme-substrate complex formed b) Substrate held in
place by hydrogen and ionic bonds 3. Active site changes shape a) Causes strain on bonds
in substrate b) A few amino acids in active site catalyzes reaction 4. Substrate converted
into product(s) 5. Products exits 6. Enzyme unchanged – can be used again G. Ways
enzymes lower activation energy 1. Bring reactants together in proper orientation 2.
Bonds in substrate distorted during induced-fit 3. Provides microenvironment conducive
to reaction a) Localized low pH b) Caused by acidic side chains 4. Side chains of amino
acids may participate in reaction
22. Explain how substrate concentration affects the rate of an enzyme-controlled
reaction.
Effect of substrate concentration on rate of enzyme-controlled reaction 1. Increase
substrate concentration – increase rate of reaction 2. If substrate level high a) Enzymes
become saturated b) Reaction rate dependent on how fast active sites convert substrate
into product
23. Explain how enzyme activity can be regulated or controlled by environmental
conditions, cofactors, enzyme inhibitors and allosteric regulators.
b) Temperature (1) Optimal temperature (2) Allows for greatest number of collisions
without denaturing enzyme (3) Humans – optimal temperature is 35oC to 40oC c) PH (1)
Optimal range 6 to 8 (2) Exception – stomach enzymes d) Ionic concentration (1) Ions
can interfere with ionic bonds within enzyme (2) Result = disrupts shape
24. Distinguish between allosteric activation and cooperativity.
Alosteric is A specific receptor site on an enzyme molecule remote from the active site.
Molecules bind to the allosteric site and change the shape of the active site, making it
either more or less receptive to the substrate. While on the other hand coopertivity is An
interaction of the constituent subunits of a protein causing a conformational change in
one subunit to be transmitted to all the others.