Bio Exam Notes
Bio Exam Notes
Characteristics of Lif
• organization
• energy us
• evolution
Chapter
Elements Are Fundamental Types of Matte
• element: pure substance that cannot be broken down by chemical means into other
substances
• bulk element: required in large amounts because make up vast majority of every living cell
• atom: smallest possible piece of an element that retains characteristics of the element
- composted of 3 particles
protons = + charge
neutrons = no charge
• all atoms of an element have same # of protons but not necessarily neutrons
• radioactive isotopes: emits energy as rays or particles when they break down into more stable
form
- every radioactive isotope has a characteristic half life which is the time it takes for half of
atoms to emit radiation or decay to a different more stable form
• energy shell: group of electron orbitals that share same energy level
- rst shell holds up to 2 elections and rest can hold up to
- # of protons = # of electron
• atoms valence shell is its outermost occupied energy cell & atoms are most stable when full
• electrons stolen/shared, transfer electrons from one atom to another creates a chemical bon
electronegativity
Ionic Bond 1 atom donates 1 or strong but easily breaks table salt (NaCl)
more electrons to in water
another atom, forming
oppositely charged ions
that attract each other
Covalent Bond two atoms share pairs strong O—H bond within H2O
of electrons molecule
• polar covalent bond: lopsided union in which one nucleus exerts a much stronger pull on the
shared electrons than does the other nucleus
carbon carbon bond, is non polar; after all a bond b/w 2 identical atoms must be electrically
balanced
• when covalent bond is polar, negatively charged electrons spend more time around the
nucleus of the more electronegative atom than around its partner
- electron hogging atom = partial negative charge and other = partial positive charg
• in hydrogen bond, opposite partial charges on adjacent molecules or w/i a single large
molecule - attract each other (atom w/ partial positive charge is H
• cohesion & adhesion - ex: water moves from plants roots to it’s leave
• regulates temperatures - ex: coastal climates = more mild than inland climate
• chemical reactant & product = ex: photosynthesis reactions require water molecule
• surface tension: liquid to hold together at it’s surface (not all liquids exhibit it
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• polar solvents dissolve polar molecules & non polar solvents dissolve non polar substances
• hydrophobic (non polar molecules): do not dissolve in or form hydrogen bonds with wate
• chemical reaction: 2 or more molecules swap their actions to yield different molecules; that is,
some chemical bonds break and new ones form
Cells Have an Optimum P
• one of the most important substances dissolved in water is one of the simplest: H+ ion
- each H+ is stripped of its electro
• one source of H+ is pure wate
- at any time, about 1 million water molecules breaks into 2 pieces —> one hydrogen ion H+
and one hydroxide ion OH- H2O —> H+ (+) OH
• buffer system: allows organisms to maintain pH w/i certain limits; pairs of weak acids & bases
consume or release H+, adding acid or base therefore doesn’t affect pH of buffered solutio
• organisms composed mostly of water and organic molecules, chemical compound that contain
both carbon & hydrogen
- lipids
Nam
Hydroxyl group
Carboxyl grou
Amino grou
Phosphate grou
Proteins polymer of amino acids carry out nearly all work of cell
Nucleic Acid (DNA/RNA) polymer of nucleotides store/use genetic info & transmit
to next generation
Steroids four fused rings, mostly C & H stabilize animal membranes; sex
hormones
Sugar
• smallest carb, the monosaccharides (sugar molecule), contain 5-6 carbon atoms
Complex Carb
• cellulose forms part of plant cell walls, humans cannot digest BUT make up much of ne
• chitin is found in cell walls of fungi, and exible exoskeletons of insects, spiders and
crustacean
• starch and glycogen both act as storage molecules that readily break down into their glucose
monomers when cells need burst of energy (most plants store starch, while glycogen occurs
in animal & fungi cells
• each amino acid has central carbon atom bonded to 4 other atoms or groups of atom
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• one is a hydrogen atom; another is a carboxyl group; a third is an amino group, a nitrogen
atom single bonded to 2 hydrogen atoms (-NH2); & fourth is a side chain or R group which
can be any of 20 chemical groups
• R groups distinguish amino acids from one another (some are acidic or basic, some are
hydrophilic or hydrophobic
- dehydration synthesis reaction connects amino acids to each other; a peptide bond is the
resulting covalent bond that links each amino acid to its neighbour
• 2 linked amino acids form a dipeptide; 3 form tripeptide, and long chains are called
polypeptide
• polypeptides called a protein once it folds into its functional shape; protein may consist of 1+
polypeptide chain
• most amino acids synthesized from scratch in humans BUT 8 are considered essential
because must come from protein rich foods; digestive enzymes catalyze hydrolysis reactions
that release them from foods, the body then uses these monomers to build polypeptides
Protein Foldin
• unlike polysaccharides most proteins don't exist as long chains inside cells, instead the
polypeptide chain folds into a unique 3D structure determined by the order & kinds of amino
acid
1. primary structure: amino acid sequence of polypeptide chain (determines all subsequent
structural levels
2. secondary structure: “structure” w/ de ned shape, resulting from hydrogen bonds b/w
parts of polypeptide, these interactions fold chain of amino acids into coils, sheets and
loops (each protein can have multiple areas of secondary structure
3. tertiary structure: overall shape of polypeptide, arising primarily through iterations b/w R
groups and water - inside a cell water molecules surround each polypeptide. The
hydrophobic R groups move away from water towards proteins interior. Hydrogen and
ionic bonds form b/w peptide backbone and some R groups. Covalent bonds b/w sulphur
atoms in some R group further stabilize the structure these disulphide bridges are
abundant in structural proteins such as keratin
- polypeptide shap
4. quaternary structure: shape arising from interactions b/w multiple polypeptide subunits of
same protein. Protein consists of 2 polypeptides; similarly the oxygen toting blood protein
hemoglobin is composed of 4 polypeptide chains
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• how does a cell “know” which amino acids to string together to form particular protein? Each
proteins primary structure is encoded in the sequence of nucleic acid (polymer consisting of
monomers called nucleotides
• dehydration synthesis links nucleotides together, in this reaction a covalent bond forms b/w
sugar of one nucleotide and phosphate group of its neighbour
• DNA’s main function it store genetic info; its sequence of nucleotides “tells” a cell which amino
acids to string together to form each protei
- not polymers consisting of long chains of monomers instead have diverse chemical
structures
Triglycerides
• consist of 3 long hydrogen chains called fatty acids bounded to glycerol, a 3 carbon molecule
that forms the triglycerides backbon
• do not consist of long strings of similar monomers, cells nevertheless use dehydration
synthesis to produce them
• enzymes link 3 fatty acids to one glycerol molecule, yielding 3 H2O molecules per triglycerid
Steroids
Chapter
Cells Are Units of Life
• cell theor
• 2 categories of life
- prokaryotes: lack a nucleus
- eukaryotes: contains nucleus and organelles further divided into bacteria, archaea and
eukarya
• bacterial cells contain nucleiod: where DNA is located and not bound by membrane
- located near DNA in cytoplasm are enzymes, RNA and ribosomes to make protein
- agella: tail helps bacteria swim/mov
- rigid cell wall surrounds cell membrane to prevent bursting if absorbs too much wate
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• archaean cells are smaller than eukaryotic cells and lack nucleus and organelles
- most have cell walls and agella
- archaea have own domain bc build cells out of biochemicals that are different from
eukaryotes and bacteria
• plant cells have chloroplasts and a cell wall which animals lac
• cytoplasm of eukaryotic cells divided into organelles that have specialized functions
• cell membrane (common to all cells) separates cytoplasm from cells surrounding
• cells surface transports substances in and out of cells and receives/responds to external
stimuli
- chemical structure gives phospholipids unusual properties in water, the phosphate “head”
end w/ it’s polar covalent bonds is attached to water (hydrophilic) and the other end
consisting of 2 fatty acid “tails” is hydrophobic
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- enzymes: proteins facilitate chemical reactions that otherwise would proceed too slowly to
sustain life
• eukaryotic cells have organelles that have specialized functions that carry out the work of the
cel
• cells internal membranes form coordinated endomembrane system: nuclear envelope, ER,
golgi apparatus, lysosomes, vacuoles, and cell membran
- connected by vesicles: small membranes spheres that transport materials inside cel
- these “bubbles” of membrane, which can pinch off from 1 organelle travel w/i cell and fuse
w/ another
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• cytoplasm includes cytosol: watery mixture of ions, enzymes, RNA and other dissolved
substance
• organelles part of cytoplasm, as are arrays of protein rods & tubules called cytoskeleton
• once in cytoplasm, mRNA coming from nucleus binds to ribosome which manufactures
proteins
• close to nucleus, membrane surface studded w/ ribosomes making proteins that enter inner
compartment of ER; proteins destined to be secreted from cell, section is called rough ER: b/c
ribosomes give these membranes rough appearance
• adjacent to rough ER is smooth ER: synthesizes lipids and other membrane components and
also houses enzymes that detoxify drugs and poisons
- lipids and proteins made by ER exit organelle in vesicles, loaded transport vesicles
pinches off from tubular endings of ER membrane and takes contents to Golgi apparatus
• Golgi apparatus: stack of at, membrane enclosed sacs that functions as a processing centre
- proteins from ER pass through series of Golgi sacs where complete intricate folding and
become functional
- enzymes in Golgi also manufacture and attach carbohydrates to proteins or lipids forming
“name tags” recognized by immune system
- Golgi sorts & packages materials into vesicles which move to cell membrane, some
proteins received from ER become membrane surface proteins; other substances are
packaged for secretion from cell
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• in milk production vesicles fuse with cell membrane and release proteins outside cell, the fat
droplet stay suspended in watery milk bc retain later of surrounding membrane when leave
cel
• besides producing molecules for export, eukaryotic cells break down molecules in specialized
compartment
• lysosomes: organelles containing enzymes that dismantle and recycle food particles, captured
bacteria, worn out organelles and debris (their enzymes cut apart substrates
- lysosomes fuse with transport vesicles carrying debris from outside of from within cel
- lysosomes enzymes break down large organic molecules into smaller subunits by
hydrolysis, releasing them into cytosol for cell to use
- some cells have more lysosomes (ex: liver so it can process cholesterol
• vacuoles: contain watery solution of enzymes that degrade and recycle molecules and
organelles
- vacuoles also contain variety of salts, sugars, and weak acids (solution is somewhat
acidic
- some protists (single cell) have vacuoles but have different functions (ex: pump excess
water out, digest nutrients
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• peroxisomes: houses enzymes that break down fatty acids and dispose of toxic chemicals
- all eukaryotic cells contain the
- originate at ER and contain different enzymes
• growth, cell division, protein production, secretion and many chemicals reactions in cytoplasm
require energy
- within matrix is DNA that encodes proteins essential for mitochondrial function; ribosomes
occupy matrix to
• cristae: folds of inner membrane and add tremendous surface area to inner membrane which
houses enzymes that catalyze reactions of cellular respiration
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Mitochondria Chloroplasts
Chapter
Energy Allows Cells To Do Life’s Work
- all chemical reactions that sustain life rely on collisions b/w moving molecules
- colder the object, slower the movement of atoms and molecules and many die if
conditions are too chilly
• 1st Law - Energy of Law Conservation: energy cannot be created or destroyed, although it can
be converted to other forms
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• photosynthesi
- plants and some microbes use carbon dioxide, H2O, and kinetic energy in sunlight to
produce sugars that are assembled into glucose and other carbohydrates and these
molecules contain potential energy in their chemical bonds
• cellular respiration
- energy rich glucose molecules change back to carbon dioxide and H2O, liberating energy
necessary to power life, cells translate some potential energy in glucose into the kinetic
energy of molecular motion and use that kinetic energy to do work
• 2nd Law of Energy Conservation: all energy transformations are inef cient because every
reaction loses some energy to surroundings as heat
- entropy: measure of the randomness (the more disordered the system is, the higher the
entropy
• even though organisms are organized (may seem to defy entropy always increases) they're
not isolated form surrounding
- instead, a constant stream of incoming energy and matter allow organisms to maintain
organization and stay alive using info in DNA
- ultimately life remains ordered and complex bc sun is constantly supplying energy to Earth
• metabolism: encompasses all these chemical reactions in cells, including those that break
down existing ones
- each reaction arranges atoms into new compounds, and each reaction either absorbs or
releases energ
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• group of proteins that are electron shuttling specialists often align in membranes
- in an electron transport chain, each protein accepts an electron from molecule before it
and passes to next
- electron transport chain: membrane bound molecular complex that shuttles electrons to
slowly extract their energ
- as result, each protein in chain is rst reduced then oxidized, small amounts of energy are
related at each step and cell uses energy in other reactions
• all cells contain maze of interlocking chemical reactions, some releasing energy and others
absorbing i
- negative charges on neighbouring phosphate groups repel one another, making molecule
unstable an therefore releases energy when covalent bonds b/w phosphates break
• when cell requires energy for a chemical reaction, it “spends’ ATP by removing endmost
phosphate group
- products of hydrolysis reaction are adenosine diphosphate (ADP), the liberated phosphate
group and a burst of energy
• reactions are fundamental to biology bc ATP is the “go between” that links reactions that
require energy input w/ those that release energ
• coupled reactions: simultaneous reactions which one provides energy that drives the other
• ATP hydrolysis is coupled to reactions requiring energy input, such as those that do work or
synthesize new molecules
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1. presence of phosphate may energize target molecule, making it more likely to bond
w other molecule
ATP energizes target molecule, making it more likely to bond with other molecule
• ex: ATP provides energy to build large molecules out of small subunits
• ATP high energy phosphate bonds make molecule too unstable for long term storage
• enzyme: organic molecule that catalyses (speeds) a chemical reaction w/o being consumed
(most are proteins, some made of RNA
- enzymes copy DNA, build proteins, digest food, recycle cells worn out parts, and catalyze
oxidation reduction reaction
• one way to regulate metabolic pathway is by negative feedback: which a change triggers an
action that reverses the change
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- as reactions products accumulate, they inhibit enzyme catalyzing reaction; reaction rate
slows or stops, but when concentration of reaction product falls, block on enzyme lifts and
cell can one again carry out reactio
- competitive inhibition: product of a reaction binds to enzymes active site, preventing it from
binding substrate (competitive bc product competes w substrate to occupy active site
• pH, salt concentration, temperature and some pharmaceutical drugs can in uence enzyme
activity
• thanks to regulation of membrane transport, interior of cell is chemically different from outside
- concentrations of some dissolved substances higher inside cell than outside an others are
lowe
• concentration gradient: solute more concentrated in one region than neighbouring region
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Mechanism Characteristics
• if substances move from area more concentrated to less concentrated area its said to be
following its concentration gradient
random molecular motive increases amount of disorder and costs needy to counter
this tendency toward disorder, however an existing concentration gradient represents
form of potential energy cells therefore spend ATP to create some types of
concentration differences which can be “cashed” in to do work
• passive transport: substance moves across membrane w/o direct expenditure of energy
- all forms of passive transport involve diffusion: spontaneous movement of substance from
more concentrated region to a less concentrated region
- diffusion represents dissipation of chemical gradient and loss of potential energy - doesn't
require energy input
1. simple diffusion
2. osmosis
3. facilitated diffusion
• simple diffusion: substance moves down its concentration gradient w/o use of transport protein
- substances may enter or leave cells by simple diffusion it can pass freely through
membran
- water will diffuse down its own gradient toward side w high solute concentration
• human red blood cells demonstrates effects of osmosis
- cell interior is isotonic to surrounding blood plasma
- isotonic: solute concentration is same on both sides of semipermeable membrane
- hypotonic environment: solute concentration lower than it is inside the cell, water moves by
osmosis into blood cell placed into hypotonic surroundings (membrane may burst since no
cell wall
- hypertonic environment: surroundings have higher concentration of solutes than the cells
cytoplasm, a cell loses water, shrivels and dies
• facilitated diffusion: membrane protein assists movement of polar solute down its
concentration gradient
- ions and polar molecules cannot freely cross hydrophobic layer of a membrane, instead
transport proteins form channels to help cross
- releases energy bc solute moves from more concentrated to less concentrated region
• simple and facilitated diffusion dissipate existing concentration gradient, however, a cell needs
to do the opposite: create and maintain concentration gradient
• active transport: cell uses transport protein to move substance against its concentration
gradient - from less concentrated to more concentrated
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- bc gradient represents form of potential energy, cell must expend energy to create it
(comes from ATP
• cells must contain high concentration of Potassium and low concentrations of sodium to
perform many function
• one active transport system in membranes of most animals cells is protein called sodium
potassium pump, which uses ATP as energy source to expel 3 sodium for every 2 potassium it
admits
• large particles must enter and leave cells with help of transport vesicle - small sac that can
pinch off of, or fuse with a cell membrane
• endocytosis: cell membrane engulfs uids and large molecules to bring them into the cell
when cell membrane indents, a “bubble” of membrane closes in on itself and resulting vesicle
traps incoming substance
• 2 forms of endocytosis
- pinocytosis: cell engulf small amounts of uid and dissolved substances
- phagocytosis: cell captures and engulfs large particles (ex: debris, cell
• vesicle fuses w lysosome where hydrolytic enzymes dismantle carg
• exocytosis: uses vesicles to transport uids and large particles out of cell
- inside cell, Golgi produces vesicles lled with substances to be secreted, vesicle moves to
cell membrane and joins with it, releasing substance
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Chapter
Life Depends on Photosynthesis
• plants are autotrophs: uses inorganic substances such as H2O & CO2 to produce organic
compounds
• heterotroph: organism that obtains carbon by consuming pre existing organic molecules
• photosynthesis: process where plants, algae, and some bacteria harness solar energy &
convert it into chemical energy
- series of chemical reactions that use light energy to assemble CO2 into glucose C6H12O6
and other carb
• visible light small sliver of much larger electromagnetic spectrum, range of possible
frequencies of radiation
- photons wavelength is distance it moves during complete vibration (shorter it is, more
energy
3. infrared radiation: longer wavelengths, too little energy per photon for use and
converted to heat immediately
• plant cells contain several pigment molecules that capture light energy
- most abundant is chlorophyll (green
- also have several types of accessory pigments: energy capturing pigment molecules other
than chlorophyll (ex: carotenoids
- chlorophyll a (blue green) & b (yellow green) absorb red and blue wavelengths bc they
re ect gree
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• most photosynthesis occurs in mesophyll: collective term for cells lling leafs interior
- contain abundant chloroplasts (40-200 per cell, 500,000 per square mm
• each chloroplasts contains a lot of surface area for reactions of photosynthesis
- 2 membranes enclose the stroma; chloroplasts uid inner region, that contains ribosomes,
DNA & enzymes
- suspended in stroma are 10-100 grana, each composed of a stack of 10-20 thylakoids
- each thylakoid consists of membrane studded with photosynthetic pigments
• anchored in thylakoid membranes are many photosystems: clustered of pigments and
proteins part of photosynthesis
- additional pigments called antenna pigments: capture photon energy and funnel it to
reaction centre
• antenna pigments capture light energy and send it to reaction centre chlorophyll which uses it
for reactions of photosynthesis
1. light reaction
2. carbon reaction
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Light Reaction
• light reactions: harvest light energy and store it in molecules of ATP or NADPH
- in chloroplasts thylakoid membranes, pigment molecules in 2 linked photosystems capture
kinetic energy from photons and store as potential energy in chemical bonds of 2
molecules: ATP & NADP
- ATP: nucleotide that stores potential energy in covalent bonds b/w it’s phosphate groups
(forms when phosphate group added to ADP
Carbon Reaction
• carbon reactions: chloroplasts uses ATP, high energy electrons in NADPH & CO2 to produce
sugar molecules
- ATP & NADPH come from light reactions & CO2 comes from atmosphere
- once inside leaf, CO2 diffuses into mesophyll cell and across chloroplast membrane into
stroma, where carbon reactions occur
• photosynthetic electron transport chain provides both the energy required for ATP synthesis &
electrons required for production of NADP
- “excited” electrons, now packed w potential energy are ejected from reaction centre
chlorophyll a molecule and begin journey through electron transport chain
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- reaction centre chlorophyll a molecule replaces electrons from water, which donates 2
electrons when splits into O2 and 2 protons (H+
- chlorophyll a picks electrons, protons released into thylakoid space and O2 used in plant
respiration or released into environment
• ATP synthase: enzyme complex that transforms the gradients potential energy into chemical
energy in form of AT
- channel in ATP synthase allows protons trapped inside thylakoids space to return to
strom
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