Bio 150 Final Exam

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257 Terms

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Properties of life
Organized complexity, metabolism, can reproduce, can respond to their environment, composed of cells
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Ions
Numbers of protons and electrons differ
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Most common elements found on earth
Nitrogen, oxygen, carbon, hydrogen
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nonpolar covalent bond
Electrons shared equally, similar electronegativity
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polar covalent bond
one atom has a much higher electronegativity
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molecule
two or more atoms held together by covalent bonds
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hydrogen bond
weak association formed between polar molecules
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cohesion
water and water
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adhesion
water and other polar molecules
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Cation
positive ion
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anion
negative ion
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Why does ice float?
It is less dense than water, H bonds cause molecules in ice to spread farther apart. This is important for aquatic organisms.
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Function groups
groups of atoms that together have specific chemical properties.
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Five functional groups
hydroxyl (-OH), carbonyl (C\=O), carboxyl(C\=O-OH) , amino(N-H-N), phosphate
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dehydration synthesis
build up polymers
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Hydrolysis
break down of polymers by addition of water
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Carbohydrates
1:2:1 ration of carbon, hydrogen, and oxygen C6H1206
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How are carbohydrates linked?
glycosidic bonds
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Function of carbohydrates
Energy source
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Carbohyrates monomer
monosaccharides (simple sugars)
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Plant and animal carbohydrates
Plants (structure and storage):starches and cellulose
Animals (structure and storage): glycogen and chitin
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Lipids
hydrophobic tails
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Lipids monomer
fatty acids
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unsaturated lipids
liquid at room temperature (oil)
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saturated lipids
solid at room temperature(fats)
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Lipids bonds
ester linkage
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Nucleic acids bonds
phosphodiester bonds
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Nucleic acids makeup
5 carbon sugar, phosphate group, nitrogenous base
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RNA
Protein synthesis
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DNA
Codes to make proteins
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Proteins makeup
Do almost everything in the cell, central C, carboxyl group, amino acid sequence, side group (r)
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proteins are linked by
peptide bonds
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protein primary structure
sequence of amino acids
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protein secondary structure
The folding of the primary structure of a protein. This folding is caused principally by hydrogen bonds.
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proteins tertiary structure
the complete, three-dimensional arrangement of a polypeptide chain
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proteins quaternary structure
2 or more polypeptides (folded in tertiary structure) linked together
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Denaturation
loss of normal shape of a protein due to heat or other factor
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Cell
smallest unit that has all properties of life
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fluid mosaic model
phospholipid bilayer with embedded proteins
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factors that affect fluidity
Warmer temps and unsaturation\= more fluid
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integral proteins
penetrate the hydrophobic interior of the lipid bilayer (amphithatic)
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passive transport
Requires NO energy, Movement of molecules from high to low concentration, Moves with the concentration gradient
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Diffusion (passive transport)
moves particles from a higher to a lower concentration
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simple diffusion
movement of a solute from an area of high concentration to an area of low concentration, small nonpolar molecules
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facilitated diffusion
Movement of specific molecules across cell membranes through protein channels
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How do polar molecules diffuse
through aquaporin channels
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Osmosis
diffusion of water towards higher solute concentration
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Isotonic
when the concentration of two solutions is the same
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hypertonic
Having a higher concentration of solute than another solution.
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Hypotonic
Having a lower concentration of solute than another solution
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How do cells react to hypertonic solutions?
Shrivel
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active transport
Energy-requiring process (ATP) that moves material across a cell membrane against a concentration difference
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bulk transport
The process by which large particles and macromolecules are transported through plasma membranes. Inc. exocytosis and endocytosis
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Prokaryotes vs. Eukaryotes
- Prokaryotes have no nucleus or membrane bound organelles
- Eukaryotes have a nucleus and membrane bound organelles
- Both can reproduce and respond to the environment
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Smooth Endoplasmic Reticulum (SER)
lipid synthesis
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Rough Endoplasmic Reticulum
protein synthesis
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Golgi apparatus
A system of membranes that modifies and packages proteins for export by the cell (FEDX)
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Lysosomes
An organelle containing digestive enzymes
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Cytoskeleton
network of protein filaments within some cells that helps the cell maintain its shape and is involved in many forms of cell movement
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Metabolism
All of the chemical reactions that occur within an organism, catalyzed by enzymes
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anabolic reactions
build up large chemicals and require energy
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catabolic reactions
break down large chemicals and release energy
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Energy
the ability to do work
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1st law of thermodynamics
Energy cannot be created or destroyed
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2nd law of thermodynamics
Every energy transfer or transformation increases the entropy of the universe.
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chemical reactions produce
heat
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free energy
energy that is available to do work
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exergonic
Chemical reactions that release energy, negative free energy, spontaneous (catabolic)
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endergonic reaction
requires energy, positive free energy, nonspontaneous (anabolic)
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ATP
(adenosine triphosphate) main energy source that cells use for most of their work
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How is energy released from ATP?
Phosphate bond broken down by hydrolysis
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energy coupling
The use of an exergonic process to drive an endergonic one.
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catalyze
enzymes speed up chemical reactions
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Substrate
The reactant that an enzyme acts on
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activation energy
the minimum amount of energy required to start a chemical reaction, enzymes reduce amount of energy required
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Competitive inhibition of enzymes
competes with the substrate to bind to the active site
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noncompetitive inhibitor of enzymes
binds to a different active sit but still has effect on enzyme, alters active site
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allosteric regulation
molecules binds to non active site and alters function of active site
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Griffith
genetic trains can be transferred between cells
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Griffith Experiment (1928)
1. Mice injected with pathogenic pneumococci (bacteria) die
2. Mice injected with nonpathogenic or dead pathogenic pneumococci are unaffected
3. Mice injected with heat-killed pathogenic bacteria and live nonpathogenic bacteria die; live pathogenic bacteria are isolated from them; these bacteria remain pathogenic in future generations

Interpretation: Live nonpathogenic bacteria have taken up some "transforming principle" from the dead pathogenic types and have been permanently transformed by it. This transformation is passed on to future generations of the bacteria.
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Avery, MacLeod, McCarty
Determined that DNA was Griffith's "Transforming Factor."
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Avery-MacLeod-McCarty experiment
isolate DNA, protein and others, mix with normal bacteria to prove DNA is transforming substance
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Chargoff's Rule
A\=T and G\=C
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Franklin
DNA shaped like helix, consistent diameter
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Watson and Crick
Developed the double helix model of DNA, sugar phosphate backbone, strands held together by hydrogen bond, strands are antiparallel
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Replication is complementary
One strand determines the sequence of its partner
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Replication is semiconservative
New DNA composed of one original and one daughter strand
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DNA synthesis
5 prime to 3 prime direction
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DNA polymerase enzymes add
new nucleotides to the existing 3 prime end of growing daughter strand
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replication fork
A Y-shaped region on a replicating DNA molecule where new strands are growing
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leading strand
synthesized continuously
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lagging strand
A discontinuously synthesized DNA strand that elongates by means of Okazaki fragments, each synthesized in a 5' to 3' direction away from the replication fork
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Helicase
unwinds DNA
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single strand binding proteins
bind to and stabilize single-stranded DNA
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Topiosomerase
relieves strain caused by unwinding
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RNA primase
makes RNA primer for DNA polymerase to start from
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Lagging strand synthesis
-RNA primer made by RNA Primase
-DNA polymerase adds nucleotides 5'
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Prokaryote DNA replication
Circular chromosomes, one origin of replication: site where replication begins
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Eukarytoic DNA replication
Long, linear
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problem for eukaryotic DNA replication
ends of linear chromosomes get shorter with each round of replication