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Biology 121

QuestionAnswer
The Cellular level atoms, molecules, organelles, cells
The organismal Level tissues, organs, organ systems
The Population Level Population, species, community
The Ecosystem Level ecosystem
Deductive reasonings principles to predict specific results
inductive reasoning specific observations to construct scientific principles
hypothesis explanation to account for observation
experiment tests hypothesis
variables something influenced by factors
test experiment one variable that is altered to test hypothesis
control experiment one variable is left unaltered
theory explanation of natural phenomenon, supported by experiments and scientific reasonings
Darwin's artificial selection breed animals for certain traits
Darwin's survival of the fittest those who adapt to survival will survive
Darwin's natural selection like artificial selection but nature does the pruning
evidence for evolution fossil record, comparative anatomy, molecular evidence
Cell theory all living things consist of cells
DNA (deoxyribonucleic acid) formed from two long chains of nucleotides which encode the cells information
gene specific sequence of several hundred to many thousand nucleotides. (a discrete unit of information)
Genome The entire set of DNA instructions that specify a cell
Eukarya Plantae, Fungi, Animalia, Protista
What are the 3 domains of the life's great diversity Eukarya, Archea, Bacteria
Electrons negative charge, outside of the atom
Protons Positive charge, inside the nucleus of atom
neutrons neutral charge, inside the nucleus of atom
atomic number is = to the number of protons
element substance that can not be broken down to any other substance by ordinary chemical means
atomic mass =p+n
weight of proton 1 dalton
location of electron orbital
neutral atoms same number of protons and electrons
ions charged particles
cations having more protons than electrons ( more positive)
anions less protons than electrons (negative)
isotope an atom of a single element that possess different numbers of neutrons
half-life decay time
oxidation loss of an electron
reduction gain of an electron
redox reactions the process of oxidation+ reduction
valence electrons electrons in the outermost energy levels
octet rule full outer energy levels (8)
molecule group of atoms held together by energy
compound a molecule that contains atoms of more than one element
chemical bonds atoms in a molecule are joined by chemical bonds.
ionic bonds atoms w/ opposite charges attract. 2nd strongest
covalent bonds two atoms share one or more pairs of electrons. Strong
Hydrogen Bond sharing of H atom. medium strength
hydrophobic interaction forcing of hydrophobic portions of molecules together in presence of polar substances. Moderately weak strength.
bonds triple bond is stronger than a double bond which is stronger than a single bond
electro negativity increases from left to right, increases from bottom to top. (upper-right hand corner of periodic table holds the most elctronegative elements.
nonpolar electrons are equally shared
polar not equally shared or more electronegativity
increases if chemical reactions temperature, concentration,catalysts
cohesive polarity of water allows water molecules to be attracted to one other.
surface tension caused by cohesion * this allows bugs to walk on top of water*
Properties of water cohesion, high specific heat, high heat of vaporization, lower density of ice, solubility.
Benefit to life: Cohesion leaves pull water upward from the roots; seeds swell and germinate
Benefit to life:High specific heat water stabilizes the temperature of organisms and the environment
Benefit to life: High heat of vaporization evaporation of water cools body surfaces
benefit to life: Lower density of ice lakes do not freeze solid, allowing fish and other life in lakes to survive the winter
Benefit to life: solubility Many kinds of molecules can move freely in cells, permitting a diverse array of chemical reactions
Adhesion attraction of other polar substances
hydration shell water molecules surrounding
hydrophobic hates water *shrink from the contact with water* are nonpolar
hydrophilic loves water, polar molecules
hydrophobic exclusion forcing the hydrophobic portions of a molecule together.
buffer minimizes change in pH
hydrocarbons molecules consisting of carbon and hydrogen
functional groups molecules C-H core to specific molecular groups
Macromolecules Carbohydrates, nucleic acids, proteins, lipids
Carbohydrates Starch, Glycogen, cellulose, chitin which are glucose
Nucleic acids DNA, RNA which are nucleotides
Proteins Functional, structural which are amino acids
Lipids Fats, phospholipids, prostaglandins, steroids, terpenes
Fats Glycerol and three fatty acids: used for energy storage
Phospholipids Glycerol, two fatty acids, phosphate, and polar R group: used for cell membranes
Prostaglandins Five-carbon ring with two nonpolar tails: used for chemical messengers
Steroids four fused carbon rings: used for membranes, hormones
terpenes long carbon chains: used for pigments, structural support
isomers same structural formula can exist in different forms
chiral mirror-image version
polymer long molecule built by linking together large number of small, similar chemical subunits called monomers
dehydration reactions long chains are built by chemical reactions *removal of -OH or -H
Hydrolysis reaction a molecule of water is added to break down
monosaccharides simple sugar. can be 3-6 carbon sugar
Glyceraldehyde 3 carbon sugar
Ribose 5 carbon sugar
Deoxyribose 5 carbon sugar
Glucose 6 carbon sugar
fructose 6 carbon sugar
Galactose 6 carbon sugar
energy storage sugars 6 carbon sugar
disaccharide made by the linking of two monosaccharides
Polysaccharides longer polymers made up of monosaccharides
Starch storage polysaccharides, insoluble
glycogen comparable molecule to starch but in animals also insoluble
nucleic acids information carrying devices of cells
DNA encodes genetic information,used to assemble proteins
RNA reads the cells DNA encoded informations and direct synthesis of proteins
Nucleotides consist of three components: five-carbon sugar, phosphate, nitrogenous base
Purines found in both DNA and RNA: adenine (A), guanine (G)
pyrimidines found in both DNA and RNA: Cytosine (C), only found in DNA thymine (T), Only found in RNA uracil (U)
base-pairing rules A can only pair w/ T (in DNA), A can only pair w/ U (in RNA), C can only pair w/ G
ATP (adenosine triphosphate) energy currency of the cell, drive energetically chemical rxns, powers transport across membrane, power movement of cells, common form of energy
NAD+ and FAD molecules function as electron carries in a variety of cellular processes
Protein functions Enzyme catalyst,defense, transport, support, motion, regulation, storage
Enzyme Catalyst speeds up chemical rxns without being consumed
Defense cell-surface receptors form the core of the body's endocrine and immune systems
Transport protein hemoglobin transports oxygen in the blood, myoglobin protein transports oxygen in the muscles and iron is transported in the blood by the protein transferrin
support keratin in hair, fibrin in blood clots, collagen in matrix of skin, ligaments, tendons, bones
motion muscles contract thru the sliding motion of two kinds of protein filaments: actin and myosin
regulation hormones
storage calcium and iron stored by binding as ions to storage proteins
amino acids proteins are linear polymers of 20 different amino acids. contain an amino group -NH2 and carboxyl group -COOH. the specific order of amino acids determines the proteins structure and function
peptide bond covalent bond that links to amino acids together
polypeptide a protein is composed of one or more long unbranched chains each chain is a polypeptide and is composed of amino acids linked by peptide bonds
structure of proteins primary, secondary, tertiary and quaternary
Primary amino acid sequence
secondary coiled into a spiral alpha helix and planar structure is Beta sheet. regular interaction of groups in the peptide backbone
tertiary final folded shaped. and also contains region with secondary structure
quaternary two or more polypeptide chains
motifs similarities between otherwise dissimilar proteins
domains proteins are functional units within a larger structure
chaperone proteins help other proteins fold correctly
denaturation proteins environment is altered, change in shape, or even unfold
proteins can be denatured by change in pH, temperature, ionic concentration
renaturation when proteins environment is normal some small proteins may refold to natural shape
dissocation subunits in quaternary structures may seperate without losing their individual tertiary structure
lipids insoluble in water, when placed in what hydrophilic heads face out and the hydrophobic tails go to the center making a ring
triglyceride fat molecule, excellent source of energy
saturated fats bonded to at least two hydrogen atoms
unsaturated fats between one or more pairs of successive carbon atoms
polyunsaturated fatty acids with more than one double bond
phospholipid complex lipid molecule, made up of a glycerol, fatty acids, a phosphate group. make up biological membranes.
Cell theory 1. all organisms are composed of cells 2. cells are the smallest living things 3.cells arise only by division of a previously existing cell
diffusion is effected by temperature, surface area, concentration, distance
as the size of a cell increases.. length of time for diffusion from the membrane to the interior of the cell increases.
resolution minimum distance two point can be apart and still be distinguished as two separate points
light microscope visible light use of two magnifying lenses
compound microscope magnifying in stages using several lenses
electron microscope employing electron beam
prokaryotic cells single circular DNA,cell wall, no distinct interior compartments, small,
cytoplasm semifluid matrix, contains sugars, proteins, amino acids.
cytoplasm difference in Eurkaryotics the cytoplasm contains specialized membrane-bounded compartments call ORGANELLES
plasma membrane separates its contents from its surroundings
ribosomes carry out protein synthesis
Gram positive thick single layer peptidoglycan (stains violet)
Gram negative multilayer cell wall (stain red because of the second background dye
endomembrane in eukaryotic cells weave thru the cell interior and by numerous organelles
central vacuole in plant cells, stores pigment, proteins, waste material
vesicles smaller sacs that store and transport materials.
chromosomes DNA is wound tightly around proteins and packaged into compact units
cytoskeleton in eukaryotic cells, is support by an internal protein scaffold
nucleus most easily seen organelle within a eukaryotic
histones the protein wrapped around chromosomes
nucleosome formed by DNA being wrapped about the histones
ribosomal RNA composed of two subunits which are composed of RNA
messenger RNA carries coding information from DNA
transfer RNA carries amino acids
endoplasmic reticulum (ER) largest of internal membranes in cytoplasm
rough ER (RER) it has pebble like bumps on it
Smooth ER (SER) network of smooth looking tubules
Golgi Body flattened sacks in the endomembrane system, they manufacture and secrete substances
golgi apparatus functions include collection, packaging and distribution of molecules synthesized at one location an
lysosomes membrane bounded digestive vesicles, they come from the golgi apparatus and they contain high levels of degrading enzymes, which catalyze & break down proteins, nucleic acids, lipids and carbs.
microbodies enzymes into microbodies is how eukaryotic cells organize their metabolism
glyoxysome prokaryotics version of the microbody
peroxisome type of microbody that contains enzymes that catalyze the removal of electronsand are associated with hydrogen atoms
vacuoles in plant cells. used for storage and water balance
tonoplast the membrance surrounding the vacuole
Mitochondria tubular, sausage shaped organelles. Power plant of the cell. sites of oxidation metabolism
chloroplast manufacture food supply. photosynthesis. make plants green.
plastids chloroplast, leucoplasts, and amyloplast
amyloplast stores starches
three types of fibers that compose the cytoskeleton actin filaments, microtubules, intermediate filaments
centrioles barrel shaped organelles. occur in pairs, located at right angles to each other by the nuclear membrane
centrosomes the region that surrounds the centrioles
cell membranes consist of four component groups phospholipid bilayer, transmembrane proteins, interior protein network, cell surface markers.
Phospholipid bilayer provides a flexible matrix with a barrier to permeability. animal cells also have chlorestrol in the membrane
transmembrane proteins proteins that float in the lipid bilayer. they allow passageways that allow substances & info. cross the membrane.
interior protein network proteins that reinforce the shape of the membrane.
peripheral membrane proteins proteins associated w/ membrane but not its structure
cell surface markers like glycoproteins& glycolipids on the surface of the cell in different forms to identify them
Protein transporters very selective, only let certain substances enter&leave the cell either thru channels or carriers composed of proteins
Protein enzymes attached to the membrane. carry out many chemical rxns on the inside the surface of the plasma membrane
Protein cell surface receptors receptors attached to the protein surface to detect chemical messages
Protein cell surface identity markers like ID tags
Protein Cell to cell proteins acting as a temporary or permanent bond to glue protein to each other
Protein attachments to the cytoskeleton anchored to the cytoskeleton by linking proteins. Their surface proteins interact with other cells
transmembrane domain membrane spanning region
passive transport substances can move in & out of the cell w/o the cell's having to expand in energy
concentration gradient ions &molecules can move thru the membrane easy. also the diff. between the conc. on the inside of membrane & outside
diffusion Molecules & ions dissolved in water these substance move from high conc. to lower conc.
channel proteins they have a hydrophillic interior that provides an aqueous channel thru which polar molecules can pass when the channel is open
carrier proteins bind specifically to the molecule they assist much like an enzyme binds to its substrate
selectively permeable channels and carriers are usually selective for one type of molecule and thus the cell membranes
ion channels hydrated interior that spans the membrane (passage of anything to do w. water)
gated channels opened or closed in response to a stimulus (stimulus chemical or electrical)
membrane potential voltage difference is an electrical potential differences across the membrane
three conditions determine the direction of net movement of ions 1. their relative conc. on either side of membranes. 2. voltage difference across the membrane & for gated channels 3. state of the gate (open or close)
faciliated diffusion carrier proteins that help transport ions, substances across the membrane.
saturation At a high concentration of proteins bound to molecules and the rate of transport is constant
faciliated diffusion has three characteristics: characteristic one 1. only transports only certain molecules or ions.
Faciliated diffusion has three charac. char. two 2. direction of net movement is determined by the relative conc. of the transported substance inside & outside the cell. the direction is always high conc. to low conc.
Faciliated diffusion has three charac. char. three 3. saturates; revelant proteins carriers are in use, increases in the conc. gradient does not increase the rate of movement
solvent water
solute substance dissolved in water
osmosis net diffusion of water across the membrane toward a higher solute concentration
hypertonic solution with high concentration
hypotonic solution w/ lower conc.
isotonic both solutions have same conc.
require ATP (active transport) diffusion, facilitated diffusion, osmosis or anything that using energy to move materials against conc. gradient
two process in bulk transport endocytosis and exocytosis
endocytosis the plasma membrane envelopes food particles and fluids
three types of endocytosis that cells use 1. phagocytosis 2. pinocytosis 3. receptor-mediated endocytosis
Phagocytosis cells take in particulate
pinocytosis cell takes in liquid
receptor-mediated endocytosis molecules are transported into cells by this
Kinetic energy energy of motion
potential energy stored energy
1st law of thermodynamics energy can neither be created nor destroyed only change to a different form
2nd law of thermodynamics transformation of P.E into heat or random molecule motion
entropy disorder in the universe; energy transformations proceed spontaneously to convert matter from more order, less stable to less ordered but more stable
free energy energy actually available to break & form chemical bonds (energy available to do work in a system)
endergonic positive. rxn requires input. R up to P. storing energy
exergonic negative. rxn releases free energy. R down to P. using energy
Activation energy extra energy needed to get an rxn started, destablizes existing chem. bonds
catalyst lowers A.E of rxn
ATP (adenosine triphosphate)structure ribose, a 5-carbon sugar, adenine, 3 phosphates
phosphate bonds to store (make bonds) to give off energy to use to break bonds. highly neg. much E is required to keep bonds together E released when 2 phos. bonds broken
ATP-->ADP+p1 energy released. ADP (adenosine diphosphate) P1 inorganic phosphate. rxn is reversible
Enzymes catalyze rxns in living cells most are proteins, lower AE, enzymes interact w/substrates
substrate molecule that will undergo a rxn
active site region of the enzyme that binds to the substrate
When a enzyme binds to a substrate.. the enzyme changes shape, producing a better induced fit between the molecules
inhibitor a substrate that bind to an enzyme & decreases its activity
metabolism total of all chemical rxns carried out by an organism
anabolism chemical rxns that expand energy to make/transform chemical bonds
catabolism reactions that harvest energy when chemical bonds are broken
biochemical pathways organizing chemical reaction in a cell. rxns occur in a cell in sequences
ligand signaling molecule
receptor proteins a molecule where the signal is bond (recieved)
cells communicate thru four basic mechanism plus they can send signals to themselves 1. direct contact 2. paracrine signaling 3. endocrine signaling 4. synaptic signaling
direct contact when cells are very close to eachother, the receptors recognize the cell
paracrine signaling signal molecules are released by cells, diffuse thru extracellular fluid to other cells
endocrine signaling released signal molecule may enter organisms circulatory system & travel thru out body. ex. hormones
synaptic signaling long fiber like extensions of nerve cells release neurotransmitters from their tips to the target cell
chemical synapse association between the neuron and its target cell
Created by: threasa.hicks
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