Sie sind auf Seite 1von 17

1

Lecture Notes
I.

II.

Scientific Method
A.
Inquiry Based based on observation
B.
Proceeds logically & serially
C.
Initiated by observation
D.
Steps:
1.
Observation of the action/change/phenomena/etc.
2.
Repeatability is the observed phenomena regular/repeatable?
i.
Only if repeatable is it possible to scientifically study the behavior
3.
Mechanism How does it work?
4.
Hypothesis: If action is repeatable & mechanism observed select hypothesis to test
i.
Principle of Parsimony the choice of the easiest hypothesis to test first (Occams
Razor)
5.
Before experimenting map out the possible outcomes
i.
Hypotheses:
a. Wrong choose another experiment
b. Right hypothesis may be a possible explanation
6.
By nature science can disprove but cannot prove
i.
There are only increasing probabilities of truth
E.
Theory as close to scientific truth s is possible
Chemical Foundations
A.
Atomic Theory protons (+), neutrons, electrons (-)
1.
Proton count = atomic number
2.
Electrons their arrangement in discreet outer shells dictate the atoms chemical
properties
3.
Atomic mass: protons + neutrons (= baryons heavy particles) (electrons have little
mass)
4.
Each proton + neutron = 1 Dalton or Atomic Mass Unit
5.
Isotope atom with the same number of protons but differing numbers of neutrons:
neutron count doesnt change the chemical properties of the element as theyre
determined by the electron arrangement and electron arrangement is determined by the
proton count
i.
Mass # = single atom weight | Atomic Wt = average of all naturally occurring isotopes
12
ii.
6 C Protons + Neutrons = 12 | Protons = 6
6.
Charges: p+ , eB.
Ion any particle with a net charge: caused by the gain or loss of electrons
1.
Cation positively charged ion
2.
anion negatively charged ion
C.
Ionic Bonds bond formed by attraction of ion charges
1.
Atoms have basic desire to complete outer shell to become chemically inert
2.
Loss of electron = + charge, gain of electron = - charge
3.
These charged particles attract and bond Ionic Bonding (ex. F- & Na+ NaF)
i.
Strength of tendency to form ionic bonds dictated by distance from center of period
tbl.
4.
Ionic bonds are not molecules instead form crystals (due to mutual attraction of all +
and atoms amongst each other)
D.
Covalent Bonds bonds sharing electrons in outer levels not gaining or losing electrons
1.
Symmetrical covalent bond (H2, O2, N2, ) has no polarity - bond shares
electrons 50:50 (diagram )

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

2
Asymmetrical covalent bond results in one atom having
larger pull on electrons, making the electrons more likely to
orbit the heavier element(s) and less likely to orbit the
lighter
element
resulting
in
polarity:
A.K.A.
electronegativity (see 1st diagram on page 2)
i.
Electronegativity having a greater tendency to pull
electrons and thus partially charge, or polarize, the covalently
bonded molecule
ii.
Ex: H2O Oxygen tends to pull electrons more strongly, so the
probability of shared electrons being in the O orbits is much more
likely and thus is electronegative
iii.
Polarity the uneven distribution of charge causing areas of molecules to become
partially () charged
E.
Polar Bonding
1.
Inter-molecular bonding = bonds between different molecules
2.
Intra-molecular bonding = bonds within the molecule itself (H & O bonds in H2O)
3.
Polarity caused bonding = Hydrogen Bonding (H2O to H2O bonds)
4.
Carbon will never form ionic bondsall C bonds are covalent and can also bond to itself
and as such is the basis for biology
Chemistry of Water
A.
Boiling = addition of enough energy to rip apart molecules hydrogen bonds
1.
Ease of breaking bonds is dictated by the electronegative strength of the molecule
2.
Surface tension is another feature of the strength of the H bonds in water
B.
Water nature is polar and thus it has attractive & repellent areas of charge
1.
These H bonds are responsible for the chemical & physical behavior results in fairly
strong bonds
2.
Has a high surface tension, demonstrating strong cohesion because of these bonds
3.
Also has a high latent heat of vaporization (high
thermal capacity)
4.
H2O good solvent for polar substances, especially
ionically bound salts (hydrophilic substances) as water
breaks apart the polar ionic bonds. (see img )
5.
Poor solvent for non-polar substances: waxes, fats, oils,
etc. (hydrophobic substances)
C.
PH Scale measure of the acidity of a system
1.
H2O = HOH has a slight tendencty to turn into H+ + OH- ions
i.
In ionic form the hydrogen is a lone proton.
ii.
H ions are the basis of all acids
+
2.
[H ] = 10-7M and [OH-] = 10-7M concentrations
3.
= -Log10 of that number, so:
i.
105 = -5 [H+] = 10-7 [H+] = 7 H = 7 (also OH = 7)
4.
Thus acid H is lower than 7, meaning an increase in H+ concentration
5.
pH 07 = acidic | pH 714 = basic
6.
Example: H2SO4: releases hydrogen into solution and thus is acidic, driving pH down
i.
NaOH similarly donates OH- into solution, removing the H+ concentration, raising pH
7.
pH of a system highly regulated
8.
Proton donors function as acid, proton acceptors function as bases: thus H+ not
necessarily needed to be added to function as acid.
Carbon Chemistry
A.
Covalent bonding only
2.

III.

IV.

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

3
B.
C.
D.

E.

F.

G.

Shares four pairs of eNaturally forms symmetrical tetrahedron


Will bond to itself, giving rise to variety of structures: methane, ethane,
propane, butane, pentane, hexane, septane, octane, nonane, etc.
1.
Can also form ringed structures: Cyclohexane, benzene ring, etc.
2.
Double bonding = ending in ene
Isomerism same molecular formula but differing
arrangements of atoms
1.
Structural Isomers
i.
C4H10 can be both butane or isobutane
ii.
C3H7OH can be propyl alcohol or isopropyl alcohol
2.
Geometric Isomoers (cis/trans) appear with double bonds only
i.
Trans have juxtaposed bonds, while cis isomers have bonds on the same
side of the double bond
3.
Stereoisomers/Enantisomers mirror images of each other
i.
Occurs when there are 4 different structures around the Carbon atom
Functional Groups
1.
Hydroxyl Groups OH group, alcohols
i.
Hydroxyl group becomes polar due to presence of O2 and is thus very soluble in H2O.
ii.
OH group adds an ol ending: methanol, ethanol, propanol, butanol, etc.
2.
Alkyl Group simple C-H based groups: methyl, ethyl, alkyl, etc.
i.
Formula is: CnH2n+1
3.
Carbonyl Group CHO
i.
Contains a double bonded oxygen at the end of a molecule
(polar)
ii.
Found in sugars, amino acids, nucleotides
iii.
An aldehyde if at end of C backbone (-CHO)
iv.
A keytone if attached to interior of C backbone (>CO)
4.
Carboxyl group COOH
i.
In amino acids, fatty acids; highly polar, tends to release H +,
functions as an acid
5.
Amino group NH2
i.
In amino acids and certain nucleotide bases
ii.
Water soluble, acts as a weak base (proton acceptor) to become NH3+ (ionized)
6.
Sulfhydryl group SH
i.
In amino acid cysteine; helps to stabilize proteins (acting as disulphide bridge SS)
7.
Phosphate group PO4-3
i.
In nucleotides (ATP), DNA, RNA, many proteins,
phospholipids, etc.
ii.
Water soluble, acidic
Organic Composition
1.
Polymer large molecule consisting of many similar bonded smaller units, or monomers.
i.
Connection of monomers: condensation/dehydration reactions
a. Dehydration/condensation reaction in which two
molecules become covalently bonded to each
other through the loss of a small molecule, usually
H2O
ii.
Disassembly of polymers: hydrolosis type of
cleavage reaction using water to split a polymer, attaching a hydroxyl group and a H

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

H.

I.

J.

atom derived from a water molecule to the exposed site. Essentially the opposite of a
dehydration reaction.
iii.
Enzymatic action assist in both hydrolysis and dehydration synthesis reactions
Carbohydrates consist of sugars and their polymers
1.
Monosaccharides the simplest sugars, usually with molecular formulas that are a
multiple of CH2O (ex. Glucose, most common monosaccharide C6H12O6)
i.
Most sugars form rings in aqueous solutions serve as major nutrients for cells
2.
Disaccharide double sugar, consisting of two monosaccharides joined by a glycosidic
linkage
i.
Ex: maltose = glucose + glucose; lactose = glucose + galactose; sucrose = glucose +
fructose
3.
Polysaccharides very large carbohydrates, joining hundreds to thousands of monomers
Biological Polymers
1.
Monomers the base, or repeating, unit
2.
Condensation, a.k.a. dehydration synthesis, reactions form most polymers from base
monomers
3.
Formation of poly-sugars (a.k.a. polysaccharides)
i.
Starch storage sugar/polysaccharide of plants made up entirely of glucose
monomers (through 1-4 linkages, number 1 C to number 4 C)
a. Because of the angles of the bonds the polymer forms a helical shape
ii.
Glycogen storage sugar/polysaccharide of animals
a. More extensively branched than that of plants
iii.
Cellulose structural polysaccharide that comprises cell walls of plant cells
a. Consists of glucose monomers, but all C-OH bonds between glucose monomers
are of the form.
b. Cell walls of plants are many parallel cellulose molecules held together by
hydrogen bonds between the hydroxyl groups of the glucose monomers (arranged
as microfibrils)
Lipids grouped together for their hydrophobic properties waxes, oils, fats, etc.
1.
Fats large molecules, but not polymers.
i.
Consist of one glycerol backbone and three fatty acids Glycerol is an
alcohol with three carbons, each bearing a hydroxyl group
ii.
Fatty acids have long carbon skeleton with a carboxyl group at one end
(thus giving it the acid
nomenclature)
iii.
Three fatty acids joined
by
ester linkage (C-O-C
bond
between the glycerols
hydroxyl group and the fatty acids carboxyl group) results in a triglyceride, a.k.a.
fat.
iv.
Ester bonds between the glycerol & fatty acids produce H 2O, and are condensation
synth.
v.
Fatty acid with no double bonds, all being single C-H bonds, is saturated
vi.
Fatty acid with double bonded C within the chain is
unsaturated (mono, poly, etc)
2.
Phospholipids
i.
Composed of two fatty acids rather than three, with the
third hydroxyl group of the glycerol molecule joined to
a phosphate group (quite polar)
ii.
Tail end of phospholipid is a fatty acid hydrocarbon,
and hydrophobic

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

5
Head end of phospholipids is very polar phosphate group, and thus hydrophilic
Steroids (sterol-based lipids) ex.
Cholesterol
i.
Comprised of C skeleton of four
interconnected rings (fig. )
4.
Waxes long chain fatty acids tightly
packed and bonded to long
chain alcohols or carbon rings. Are
malleable and hydrophilic.
Proteins
A.
Amino acid an amino group (-NH 3+), a carboxyl group (-COO-), the H+ atom, and one or
more atoms called its R group
1.
Amino acids are the monomers that polymerize into protein polymers
2.
21 amino acids of human biological concern
3.
Bonds between amino acids are peptide bonds ( CNC bonds, like esters but using N)
i.
Dehydration synthesis/condensation reaction joins the amino acids
ii.
Grouping of multiple amino acids is a polypeptide (chain)
iii.
In peptide bond production there is always a carboxyl group (COOH) at one end and a
nitrogen (-NH2) left over at the other C terminus & N terminus
B.
Structure
1.
The sequence of amino acids in the polypeptide chain is the Primary Structure
2.
Secondary Structure is the regular H bonding in the chain, resulting in either helix or
pleated sheet
3.
Tertiary structure domain formation, irregular bonding from Hydrogen bonds, disulfide
bridges (of the sulfhydryl group), ionic bonding and hydrophobic interactions
4.
Quaternary structure the final structure of the polypeptide chain, which determines the
function of the protein.
C.
Denaturation
1.
Any change or disruption of the 4th protein structure (change of heat, pH, etc) disables the
protein from doing its job
D.
Nucleotides
1.
All nucleotides comprised of a sugar-phosphate backbone and one nitrogenous base
i.
ATP contains three phosphate groups attached to its sugar.
ii.
Because the phosphate groups are very polar the release of those
bonds is extremely exegetic
2.
Nucleic Acids
i.
Formed by nucleotide monomers covalent bonds form between the sugar of one
nucleotide and the phosphate group of the next
ii.
DNA
a. made up of 4 deoxyribonucleotide monomers (the nitrogenous bases are what
differentiate them) Adenine, Guanine, Thymine, Cytosine
b. pentose (5 C sugar) bonded to nitrogenous base (AGTC) and to phosphate group
c. DNA contains the instructions for day to day operation and reproduction of the
cell
d. Secondary structure of DNA, formed by H bonding, is what forms the double
helix
iii.
RNA composed of ribonucleotide monomers
a. Single stranded integral in protein synthesis
b. Substitute thymine base of DNA for uracil base
iii.

3.

V.

VI.

Cell Theory
A.
Cell functional unit of all living things the smallest unit with the properties of life
1.
All have a region of DNA, all have cytoplasm, all have plasma membrane
B.
Types
1.
Prokaryotic primitive cells no membranous fixed inner structure or nucleus

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

6
Eukaryotic has a true nucleus and is a more complex cell. Plant & animal cells are
eukaryotes
Cell Structure General Cellular Parts
1.
Plasma membrane selective barrier allowing passage of oxygen, nutrients and waste to
cell
i.
Consists of a lipid bilayer that selectively prevents water
soluble substances from crossing
2.
Nucleus contains the DNA of eukaryotes directly
communicates with the (rough) ER
i.
Nucleolis mass of proteins & copies of genes coding for
ribosomal RNA
3.
Nucleoid region of cytoplasm in prokaryotes containing
DNA
4.
Endoplasmic Reticulum (ER)
i.
Smooth ER assists in the packaging and transport of materials in the cell
ii.
Rough ER contains protein clumps (ribosomes) on membrane wall, synthesizes
lipids,
5.
Ribosomes contained on wall of rough ER and in cytoplasm assist in
TRANSLATION of proteins
6.
Mitochondria primary ATP manufacturer of the cell (thus powerhouse) have their
own DNA and divide on their own
7.
Golgi Body manufacture & packaging of inner & extra cellular materials (proteins &
lipids)
8.
Vesicles membrane bound grouping of cellular material act as cellular material
transporters
i.
Lysosomes type/subset of vesicle that can open up and release digestive enzymes
breaking down cells
ii.
Peroxisomes hold enzymes for digesting fatty acids, amino acids and H2O2
9.
Chloroplasts (plant cell) photosynthetic cell, transfers sunlight & water into ATP
10.
Central Vacuole (plant cell) stores amino acids, sugars, ions and waste, takes up 50 to
90% of the plant cell interior
11.
Cytoskeleton structurally supports, gives shape to and moves eukaryotic cell (not
present in prokaryotes)
i.
Microtubules largest skeletal elements, regulates cell organelle placement and
movement
ii.
Microfilaments smallest skeletal elements, reinforce cell shape, reconfigure surface,
etc
iii.
Intermediate filaments mid sized elements, help reinforce the nucleus
2.

C.

VII.

Biological Membranes
A.
Composed of Phospholipid Bilayer
1.
One polar head, two non-polar tails (heads hydrophilic, tails hydrophobic)
2.
Highly polar objects cannot pass through bilayer because of hydrophobic tails
3.
Large molecules cannot pass through
4.
Gasses CAN pass through via Diffusion O2, Limited amount of H2O, small non-polar
organics
B.
Trans-membrane proteins can extend though the membranes
1.
Transporter membranes are thus trans-membrane proteins
i.
Surface Proteins Adhesion, Acceptor, Recognition, Communication, Transport
C.
Dynamic Fluid Mosaic The lipid bi-layer in which complex structures move (in constant
motion thus dynamic)

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

7
Transport Proteins:
Passive Transport only driving force is natural molecular movement (from high to low
concentration).
i.
Facilitated Diffusion protein whose job is to allow molecules through membrane,
from high to low concentration
ii.
Aquaporins specific transport proteins that allow H2O to pass
iii.
Ion-selective channels may be gated (controlled by chemical or voltage changes)
iv.
Gas & H2O only diffuse no active pumping
v.
Osmosis Diffusion of H2O across a semi-permeable membrane
a. Osmotic Pressure = Turger Pressure
b. Tonicity concentration of solute
2.
Active Transport can move molecules from low to high concentration but requires
energy to do so
i.
Primary active transporters get energy from cleavage of ATP; pump molecules
against a concentration gradient via ATP-ase activity | always have 2 binding sites,
one for ATP, other for transport of substrate
ii.
Secondary active transporters co-transporters use energy from the gradient (ex.
Mitochondria) as energy is released from one gradient it is used to pump against
another
iii.
C/ X gradient difference in concentration/distance = the shorter the distance
needed to travel, the faster the rate of diffusion
3.
Bulk Transporters All membrane mediated
i.
Exocytosis cell excretory function
ii.
Endocytosis intake of cellular material (how amoebae feed)
iii.
Phagocytosis Solids ingestion of material by a cell for nutrition or distribution
iv.
Pinocytosis Liquids droplets of liquid ingested by cell
Bio-Energetics transformation of energy in living things
A.
Energy the capacity for doing work
B.
Work exertion of a force through a distance
C.
1st law of Thermodynamics Energy can neither be created or destroyed, only
transferred/changed state
D.
2nd law of Thermodynamics All energy put into a system cannot be extracted. No system
is 100% efficient (entropy). Amount of wasted energy = efficiency of a system
E.
Potential/Kinetic Energy
1.
Potential: Chemical, Mechanical, Gradient, Electrical every gradient has PE (battery)
2.
Kinetic Energy KE = 1/2MV2
i.
Molecular KE thermal energy, a.k.a. Heat heat = # of molecules x average KE of
the molecules; temperature is the measure of the average KE of a system
3.
Energy diagrams C6H12O6 + 6O2 6CO2 + H2O + Energy (ATP)
F.
Enzymes proteins that are used to lower the activation energy required to start a reaction
1.
Change ONLY rate at which reaction occurs nothing else
G.
Reaction Participants:
1.
Reactant Starting Agent (A & B)
2.
Product Result of reaction (C & D)
3.
Substrate material binding to enzyme before reaction (A & B)
4.
Intermediate Partial steps in Reaction
5.
Enzyme Biological catalyst (e1)
6.
Cofactor (co-enzyme) additional compound needed to assist enzyme in lowering
activation energy (Mg++ or B12)
H.
Oxidation/Reduction reactions
D.

1.

VIII.

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

8
Oxygen Family IV loss of e - makes oxygen oxidized (any loss of e-, not necessarily
oxygen)
2.
Gain of e- = reduced
3.
NAD NADH = Reduced | NAD+ = Oxidized
I.
Metabolic pathways can be linear, cyclical or branched
J.
Reversibility of reactions A B
1.
Reactions tend to flow in direction that releases lots of energy
i.
Concentration Equilibrium: Keq = [B]/[A]
2.
LeChatilers principle stressing a system in equilibrium shifts the balance in the
opposite direction until equilibrium is established
i.
Ex. A + B C + D (+ energy)
a. If: concentration of A, reaction speeds up, concentration of B,C, D
K.
Enzyme function only effect rate of reaction
1.
Induced Fit Model: Warping of enzyme by substrate binding changes energy relationships
in the substrate, thus lowering activation energy changing of substrate into product(s)
after reaction causes attraction between enzyme/reactant to cease
2.
temperature activity (slower molecules)
3.
temperature activity (until quaternary structure becomes denatured)
4.
pH free H+ effects H bonds in tertiary or quaternary structure thus have a pH optimum
L.
Control of Enzyme Activity
1.
Allosteric Activation/Inhibition Binding of a second molecule to a 2 nd binding site on
the enzyme increasing/decreasing enzyme activity
2.
Competitive Interference/Inhibition process in which
competitor binds to active site on the enzyme and prevents
substrate from being acted upon by enzyme
3.
Feedback Inhibition The process by which the products of a
reaction shut down the original reaction:
i.
Allosteric can turn on & off enzymatic action
ii.
Competitive can only make enzymatic action more
difficult
Energy Releasing Mechanisms
A.
Anaerobic O2 not required
1.
Glycolysis
i.
Alcoholic Fermentation Yeast CO2 + Ethanol (ethyl alcohol)
ii.
Lactate fermentation complicated animals lactic acid formed
iii.
Excretion of toxins in anaerobic pathways
B.
Aerobic respiration
1.
Glucose as common metabolite available from
foods, converted from other monosaccharides,
cleaved from disaccharides, glycogen & starch
2.
C6H12O6 + 6O2 6CO2 + 6H2O + ATP (max yield
of 36 ATP) via one of two pathways glycolysis &
oxidative phosphorylation
i.
Glycolysis
a. The anaerobic phase: Each glucose produces
2 pyruvate molecules
b. For each glucose 2ATP must be used to diphosphorylate the glucose
c. 4ATP are produced resulting in net gain of
2ATP
1.

IX.

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

9
3.

4.

d. Energy associated with the hydrogen carried on 2 NADH carriers


Preparatory steps to the Krebs Cycle (TCA, Citric Acid Cycle)
i.
The two (3-carbon pyruvates) are converted to two (2-carbon) activated acetylCoenzyme-A complexes
ii.
This produces two CO2 molecules as by-product
iii.
And releases the energy of two NADH carriers
iv.
This prepares the Acetyl-CoA for entry into
the Krebs cycle
Krebs Cycle cyclic pathway that takes in the 2carbon Acetyl CoA and removes its carbons,
hydrogens and electrons
i.
Products are 2CO2, 3NADH, FADH2 and an
ATP by substrate level phosphorylation
ii.
Cycle
cranks
twice for
each
glucose
that
enters
iii.
Takes
place in
the
mitochondrial inner compartment
5.
Oxidative (Electron transfer) Phosphorylation
occurs through action of transmembrane enzymes in the cristal of the mitochondria
Uses energy from H+ and their associated electrons brought by the carriers NADH and
FADH2
i.
Chemiosmosis ability of certain
membranes to use chemical energy to pump
hydrogen ions and then harness the energy
stored in the H+ gradient to drive cellular
work (ATP synthesis) in this example:
turns 2NADH & 2 pyruvates from
glycolysis into 2FADH2 & 2 Acetyl-CoA
ii.
NADH & FADH2 give up their electrons,
which power H+ pumps pushing the free
hydrogen outside the mitochondrial matrix
this forms an electrical & concentration
gradient of H+ ions. These H+ ions flow
back through ATP synthase, powering ADP + Pi ATP
iii.
Oxygen is the final e- acceptor, without which the entire process backs up to the
pyruvate, forcing the system into anaerobic respiration as lactate (as pyruvate
lactase, via LDH)
iv.
Energy from 1 NADH in Krebs 3 ATP | 1 FADH2 = 2 ATP
v.
Thus in aerobic respiration: 1 molecule glucose = Glycolysis SLP. 2 ATP, Krebs
SLP. 2 ATP, 6NADH in Krebs 18 ATP, 2NADH from glycolysis 4 ATP,
2FADH2 from Krebs 4 ATP, 2NADH in pyruvate to Acetyl CoA stage 6 ATP = 36
total ATP

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

10
Lecture Notes III
X.
Energy Releasing Mechanisms
A.
Anaerobic O2 not required
1.
Glycolysis
i.
Alcoholic Fermentation Yeast CO2 +
Ethanol (ethyl alcohol)
ii.
Lactate fermentation complicated animals
lactic acid formed
iii.
Excretion of toxins in anaerobic pathways
B.
Aerobic respiration
1.
Glucose as common metabolite available from
foods, converted from other monosaccharides,
cleaved from disaccharides, glycogen & starch
2.
C6H12O6 + 6O2 6CO2 + 6H2O + ATP (max yield of 36 ATP) via one of two pathways
glycolysis & oxidative phosphorylation
i.
Glycolysis
a. The anaerobic phase: Each glucose produces 2 pyruvate
molecules
b. For each glucose 2ATP must be used to di-phosphorylate the
glucose
c. 4ATP are produced resulting in net gain of 2ATP
d. Energy associated with the hydrogen carried on 2 NADH
carriers
3.
Preparatory steps to the Krebs Cycle (TCA, Citric Acid Cycle)
i.
The two (3-carbon pyruvates) are converted to two (2-carbon) activated acetylCoenzyme-A complexes
ii.
This produces two CO2 molecules as by-product
iii.
And releases the energy of two NADH carriers
iv.
This prepares the Acetyl-CoA for entry into
the Krebs cycle
4.
Krebs Cycle cyclic pathway that takes in the 2carbon Acetyl CoA and removes its carbons,
hydrogens and electrons
i.
Products are 2CO2, 3NADH, FADH2 and an
ATP by substrate level phosphorylation
ii.
Cycle
cranks
twice for each
glucose
that
enters
iii.
Takes place in
the
mitochondrial
inner
compartment
5.
Oxidative (Electron
transfer)
Phosphorylation
occurs through action of transmembrane enzymes in

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

11

XI.

the cristal of the mitochondria Uses energy from H + and their associated electrons
brought by the carriers NADH and FADH2
i.
Chemiosmosis ability of certain membranes to use chemical energy to pump
hydrogen ions and then harness the energy stored in the H+ gradient to drive cellular
work (ATP synthesis) in this example: turns 2NADH & 2 pyruvates from
glycolysis into 2FADH2 & 2 Acetyl-CoA
ii.
NADH & FADH2 give up their electrons, which power H + pumps pushing the free
hydrogen outside the mitochondrial matrix this forms an electrical & concentration
gradient of H+ ions. These H+ ions flow back through ATP synthase, powering ADP
+ Pi ATP
iii.
Oxygen is the final e- acceptor, without which the entire process backs up to the
pyruvate, forcing the system into anaerobic respiration as
lactate (as pyruvate lactase, via LDH)
iv.
Energy from 1 NADH in Krebs 3 ATP | 1 FADH2 = 2
ATP
v.
Thus in aerobic respiration: 1 molecule glucose =
Glycolysis SLP. 2 ATP, Krebs SLP. 2 ATP, 6NADH
in Krebs 18 ATP, 2NADH from glycolysis 4 ATP,
2FADH2 from Krebs 4 ATP, 2NADH in pyruvate to
Acetyl CoA stage 6 ATP = 36 total ATP
DNA Replication (Experiments)
A.
Frederick Griffith realized there
was a transfer of genetic material
from one strain of bacteria to
another strain:
1.
Mouse bacterial infection:
2.
Concluded living avirulent strain takes in the gene for
production of smooth coated bacteria that is virulent:
Thus the rough coated
(avirulent)
bacteria
is
TRANSFORMED
into
smooth coated (virulent)
B.
Hershey-Chase Experiments
Questioned: What is the genetic material being transferred
1.
Used bacteriophage virus consisting only of a protein coat
and a DNA core
2.
Used radioactive isotopes of Sulfur (present only in the
protein coat) and Phosphorus (only present in DNA) to
determine whether the genetic information was in the
protein, the DNA or both.
3.
Determined it was the DNA which carried the genetic
material.
C.
Watson, Crick, et. Al. (especially Franklin)
1.
Determined,
through
X-ray
crystalography
and
advanced
mathematical calculations that DNA is
shaped in a double helix. (Strands are
antiparallel)

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

12
Double helix consists of alternating phosphate-sugar
rails with nitrogenous base rungs
i.
Adenine/Guanine Purines (double ringed bases)
ii.
Cytosine/Thyamine Pyrmidines (single ringed bases)
iii.
C/G 2 Hydrogen bond attachment, A/T 3 H bond
attachment
3.
Chargaffs Rules: States that A/T, G/C must form rails
in the double helix; the double rings are each matched
with a single ring.
DNA Replication: (Chs 13/14)
A.
Meselson & Stahl Now that DNA is known to be the
purveyor of genetic information being passed on, how is DNA
replicated?
1.
3 Models from which to chose; conservative, dispersive & semiconserv.
2.
Parent generation grown in heavy nitrogen (N15)
while subsequent R1 & R2 generations grown in
ordinary nitrogen (N14)
3.
R2 Generation then centrifuged to find out where the
DNA would end up, telling them which model was
correct. (All at the same place for dispersive, two
places in R1 for conservative, two distinct places in
R1 for semi-conservative)
B.
Ribose/Deoxyribose:
1.
Deoxyribose has only an H at the 2C instead of an OH.
2.
Ribose has an OH on the 2 C
3.
Notice: 3 & 5 Carbon attachment sites along which replication
occurs:
i.
End of DNA rail is the 3 end sequence is 3C-P-5C-P-3C-P5C-P-3C...
2.

XII.

C.

distinct
R2 but not

Activity at replication (replication fork all takes place during STAGE S of interphase)
Helicase activity unwinds the double-helix prior to replication
(at the V of the fork)
2.
Complex enzyme DNA polymerase unwraps DNA & begins
assembling along leading strand
i.
DNA polymerase is only able to build new DNA in
direction from 3 to 5 along the parent strand.
a. DNA polymerase releases two phosphates from a free
floating nucleotide base.
b. Energy released by this drives the attachment of the
remaining P to an OH hanging off the 3 C sugar of
the preceding rung
ii.
Thus, one strand can be replicated smoothly (leading), the
other strand cannot (lagging)
3.
A chunk of RNA Primer attaches along the 2nd parent (lagging) strand
i.
RNA primer attaches to the lagging strand, allowing DNA polymerase to build
chunks of DNA along that strand.
ii.
These chunks being build from RNA primer by
DNA polymerase are Okazaki fragments
1.

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

13
Okazaki fragments sewn together by DNA ligase
The DNA contains an initiation and termination site, allowing mRNA to know where
to start & stop
4.
After this ligase sewing action there are two strands of DNA coming out of the S phase
as sister chromatids
DNA Repair
1.
Conducted by specialized ligases and polymerases
2.
Failure of these repair mechanisms is thought to be a cause of aging
Use of DNA information in the cell:
1.
Can only be done in G1 & G2 as DNA cannot control the functions of the cell while it is
replecating or condensed into chromosomal form.
2.
Use of the DNA material in the cell requires reading the language of DNA and
iii.
iv.

D.

E.

translating it into the language of protein structure


XIII.

Transcription/Translation
A.
Transcription the production of mRNA in nucleus. mRNA then leaves the nucleus,
traveling to the ribosomes (in the rough ER), where Translation occurs.
1.
Translation the production of polypeptide chains at the ribosomes
B.
Classes of RNA
1.
mRNA (messenger) Carries the coding sequence to build a protein.
2.
rRNA (ribosomal) Major structural elements of ribosomes. Along with proteins rRNA
molecules make up the ribosomes on which protein synthesis occurs
3.
tRNA (transfer) Specialized RNA molecules that deliver specific amino acids to the
ribosomes for insertion into a growing polypeptide (protein) in the sequence specified by
the mRNA
4.
All transcribed from DNA, thus all produced in the nucleus
C.
Transcription Process Initiated at a promoter; a base sequence on the DNA which signals
the start of a gene
1.
Differs from DNA replication in 3 ways:
i.
Only part of one DNA strand, not the whole molecule, is unwound and used as the
template
ii.
The enzyme RNA polymerase, not DNA polymerase, adds ribonucleotides one at a
time to the end of a growing strand of RNA
iii.
Unlike DNA replication, transcription results in a single unbound strand of RNA, not
a H bonded double strand of DNA.
2.
Initiated at promoter RNA polmerase enzyme mRNA molecule complementary to
the DNA base sequence
3.
mRNA must go through a maturation process before serving as a template for protein
production
i.
Non-coding portions of mRNA (introns) are enzymatically snipped out
ii.
A tail and a cap are also attached to the mRNA that help it function at the ribosome
D.
Translation Process
1.
After maturation, mRNA travels along ER to the ribosome where it serves as a template
for protein manufacture
i.
Transcription produces the mRNA whose nucleotide base sequence tells the
ribosome what the amino-acid sequence should be. The amino acid sequence
determines the (primary) structure of the protein. Primary structure of protein
determines quaternary structure of protein, which determines function.
2.
Nucleotide base sequence on the mRNA is read three at a time (triplet code or CODON)
i.
Because there are 4 bases at each position and 3 positions in a codon, there are 4 3= 64
possible codons, but only 21 different amino acids produce all proteins in the human
body.

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

14

XIV.

a. AUG start codon | UAA, UAG & UGA serve as stop codons
b. Thus 60 codons left over allowing some codons to code for the same amino-acid.
c. This phenomena is knows as Wobble Effect
3.
tRNA specific to 3 complementary base sequence found
on mRNA in ribosome AND contains an amino-acid
binding site, thus: a specific amino-acid is linked to tRNA
that is specific to the nucleotide base sequence. (tRNAs
complementary base sequence allowing attachment and
addition of amino acid known as ANTICODON)
4.
After tRNA attaches its amino acid, it leaves the ribosome
re-entering the cytoplasm pool of amino-acids to reattach
the appropriate amino acid to its specific bonding site
5.
Ribosome itself consists of two subunits (Large & Small)
i.
These subunits of the ribosome are assembled in the
nucleus and transported separately to the cytoplasm
where they are assembled and attached along the
rough ER
E.
3 Stages of Transcription
1.
Initiation - Initiator tRNA binds to a small ribosomal
subunit, creating a small subunit/tRNA complex
i.
tRNA/subunit complex attaches to mRNA
ii.
The start codon matches up with the initiator tRNA anticodon
iii.
The large ribosomal subunit joins and initiation comples
2.
Elongation the next tRNA (after the previously mentioned initiator tRNA & mRNA
trans.) with its matching anticodon loads onto the second (A) site of the ribosome and
the mRNA transcript is advanced forward one codon in the ribosome leaving the most
recently attached tRNA at the first attachment site (P) and an open second attachment site
(A) on the ribosome
i.
Now the next tRNA with its attached amino acid can link with the mRNA transcript at
the A site
ii.
Peptide bond between the two amino acids at the P and A sites is created, elongating
the polypeptide
iii.
The process then repeats
3.
Termination stage in which a stop codon moves onto the platform.
i.
Stop codon triggers the release of the protein and the mRNA from the ribosome
ii.
mRNA can be used to generate another protein molecule or broken down to make
another mRNA transcript
Chapter 11 Genetics
A.
Mendel Using pea plants found indirect but observable evidence of how parents transmit
genes to offspring
1.
Mendel was able to track the traits of his pea plants and was able to discern the patterns
showing clearly observable patterns tracing the inheritance of traits
B.
Basic Genetics:
1.
P1 = Parent Generation | F1 = first generation offspring | F2 = 2nd generation offspring
2.
Monohybrid cross = AA x aa | Dihybrid cross = AABB & aabb = AB x ab
3.
Genotype genetic composition | Phenotype observed condition/composition
4.
Rh factor in human blood (+ or -) signifying the presence of absence of the Rh or D
antigen in the blood. Rh negative mother having an Rh + child can develop antibodies
against Rh+ and eventually destroy those cells.
5.
Complete dominance = RED x white = RED | Incomplete = RED x white = Pink (because
of multiple alleles coding for the same trait)

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

15
XV.

Structural Heirarchy
A.
Cells Tissues Organs Organ Systems Organism
B.
Tasks of Physiology Maintenance of homeostasis, acquisition of O2 & nutrients, excretion
of waste, protection from attack/injury/disease, reproduction
C.
Tissues
1.
Epithelial exposed to outside, surface covering (skin, trachea, etc), can be glandular
2.
Connective Living Cells in a non-living matrix that the living cells themselves secrete
3.
Muscle contractile tissue
4.
Nerve Rapid & specific communication
D.
Cell Junction Types
1.
Tight Junctions Isolate deeper layers of a tissue from the surface
i.
Layers of protein fibers act to hold cells together make it difficult for objects at
surface to work their way between the cells into deeper tissue layers (Gut, trachea,
bladder)
2.
Adhering Junctions Great physical strength holding cells together | Cells held together
by protein plaque (Muscle, skin, tendons, etc)
3.
Gap Junctions rapid ion transfer between cells (allows for carrying of electrical signal
through tissue ) allow polar ions to pass through cell membrane (heart)
E.
Epithelium
1.
Apical at top | Basal at bottomusually rests on a basement membrane which glues
epithelium in place
2.
All epithelium is avascularblood supply is in the basement tissue
3.
Subclasses of Epithelium
i.
Lining/Surface Gut, Respiratory tract,
Urniary Tract
ii.
Glandular All exocrine glands; sweat, acid
producers in stomach, bile in liver, etc
4.
Cell Shapes
i.
Squamous (flat) Designed to reduce friction
and often to be worn away. Provides for a
large surface area and thus easily diffuses
ii.
Cuboidal Large internal volume often
have many mitochondria and golgi bodies.
High producers & metabolically active
iii.
Columnar have an apical and basal surface:
apical sometimes has cilia on it, large cellular
volume and are good secretory cells
iv.
Cells may be in a singler layer (simple) or
stacked (stratified)
F.
Connective Tissue
1.
Large variety of tissue types and levels of vascularity
i.
Avascular (cartilage) to highly vascular (bone)
2.
All characterized by having living cells suspended in a non-living matrix which the cells
themselves produce
3.
Dense Irregular Connective Tissue: Human Skin, intestinal muscles, etc; matrix packed
with many fibroblasts and collagen fibers.
4.
Dense Regular Connective Tissue: Orderly rows of fibroblasts between parallel, tightly
packed bundles of fibers. (Tendons and ligaments)
5.
Loose connective tissue (ex. Dog Skin): Framework tissues for many organs and tissues
(matrix often semi-fluid)
6.
Specialized Connective Tissues

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

16
Cartilage chondroblasts secrete a matrix which is hyaline, avascular. Rubbery,
compression resistant
ii.
Bone Osteocytes work to maintain a calcium phosphate and collagen matrix
iii.
Adipose fat tissue, used as an energy reservoir
iv.
Blood* - Living cells in a plasma matrix [dont entirely fit the description perfectly as
plasma isnt made by the blood]
Muscle - Can be very long & skinny cells
1.
Skeletal (voluntary) Striated, electrically insulated cells clustered in motor units
activated by a motor neuron. Rapid contraction and relaxation. Multi-nucleated
(therefore cannot mitose) to control action over the long length of the entire cell
2.
Cardiac Striated, branched cells, joined by gap junctions. Slower than skeletal muscle
but still rapid (<1 second). No motor neurons, no motor units. Much smaller than
skeletal muscle, single nucleus.
3.
Smooth Involuntary: non-striated. Muscle of internal organs, arterial walls, sphincters,
internal muscles of the eye. Slow gradual relaxation. Capable of sustained (over multiple
hours) contraction
Neurons (Nerve Cells)
1.
Contain an input reigon and an output reigon.
2.
Do not mitose
3.
Electrically responsive: maintain a resting electrical gradient across the membrane
4.
Consists of: Cell body, Receptive area (dendrite), and transmission reigion, usually a long
axon.
5.
Electrical Chemical Electrical charges
6.
Transduction at the synapse ensures one-way transmission; permits integration
Germ Layer Fates
1.
Endoderm Lining of respiratory and digestive tracts (pancreas, liver, etc)
2.
Mesoderm Skeletal muscle, outer covering of internal organs, blood vessels & heart,
notochord
3.
Ectoderm

all
nervous
tissue,
epidermis, skin and
hair epithelium, inner
ear, retina of eye, etc.
Started out ou outside
of blastula and migrated inward during development
Human Organ Systems
1.
Integumentary Skin and associated organs | Skeletal | Muscular | Nervous | Endocrine
General chemical signaling| Cardiovascular | Lymphatic immuno-related & returns
fluids to blood stream | Respiratory | Digestive | Urinary | Reproductive
Cavities of the Human Body
1.
Dorsal Contains cranial & spinal cavities
2.
Thoracic Contains pleural spaces (lungs) and mediastinum (heart, trachea, esophagus,
etc)
3.
Abdominopelvic From the diaphram down (stomach, liver, intestines, bladder, etc)
Planes/Positions of the Body
1.
Anterior/Posterior front/back
2.
Superior/Inferior above/below
3.
Dorsal/Ventral top/bottom of 4 legged animal (fish)
4.
Distal/Proximal far/close with respect to body attachment (extremities)
5.
Medial/Lateral close/far with respect to the trunk
6.
Transverse Cross-section at waist
i.

G.

H.

I.

J.

K.

L.

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

17
Frontal Plane Shoulder to shoulder, parallel to width of body. (Coronal when referring
to the head)
8.
Saggital Plane Division into left and right sides along the symmetrical axis (midsaggital)
M.
Homeostasis active maintenance of a constant internal environment
N.
Feedback
1.
Negative Feedback Loop Inverse relationship: fall in temp/pH = response = rise in T/pH
i.
Components: Sensor to determine the controlled variable, controller/integrator to
connect sensor to effector, effector which affects the controlled variable
ii.
Set point the level that is maintained
2.
Positive Feedback Loop Direct relationship: rise in tepm/pH = response = further rise
i.
Ex: Contractions at childbirth, nerve firing, etc
3.
Negative feedback loop allows for the maintence of stablity provided the disturbance is
not too large and overpowering for the functional response mechanisms
Nerve Cells Ch. 34
A.
Structure:
1.
Input zone: dendrites, cell body
2.
Couducting zone: Axon
3.
output zone: Axon endings (terminals)
B.
Transduction: Transfer of signal from one form to
another:
1.
Chemical electrical Chemical
2.
(input/trigger) (axon) (output zone)
C.
Ionic Distribution across cell membrane results in
most cells carrying a slight negative charge
1.
Neuron Cell Membrane: selectively permeable, depending upon charge/size, etc.
i.
Either active or passive channels (leakage channels)
2.
Membrane potential the electrical charge generated by the slightly negative charge
inside the cell compared to the outside of the cell
3.
A change in voltage opens some of the selective (active) channels
7.

XVI.

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:


JULEUS CESAR M. CADACIO, RN, RPT

Das könnte Ihnen auch gefallen