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Biology for Today Exam #2 Chapters 4-6

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Proteins   macromolecules; polymers made of covalently linked monomers (amino acids)  
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Amino Acid   organic molecule with both an amino group and a carboxyl group; monomers that make up proteins  
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What changes from amino acid to polypeptide?   the amino acid backbone  
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Peptide bond   special type of covalent bond formed by dehydration synthesis between 2 amino acids  
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dipeptide   a pair of amino acids linked by a peptide bond  
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polypeptide   long chain (polymers) of amino acids linked by a peptide bond  
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Primary Structure of proteins   linear sequence of amino acids where each amino acid is linked by a peptide bond  
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Secondary Structure of proteins   alpha-helix beta-pleated sheet  
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Tertiary Structure of proteins    
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Quaternary Structure   when several polypeptides interact with each other  
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Collagen   fibrous protein composed of long peptide chains woven together to form fibers  
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Keratin   fibrous, structural protein found in scales, horns, wool, nails and feathers  
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Silk   fibrous protein  
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Globular proteins   includes enzymes, antibodies, etc.  
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RNA   ribonucleic acid  
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DNA   deoxyribonucleic acid  
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Replication   DNA synthesis  
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Transcription   RNA synthesis  
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Translation   protein synthesis  
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Nucleotides   monomers of nucleic acids  
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Robert Hooke   first to visualize the cell in 1665  
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Antoni van Leewenhoek   first to visualize a living cell in 1674  
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Matthew Schleiden   proposed all plants are composed of cells in 1838  
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Theodor Schwann   proposed all animals consist of cells in 1839  
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Rudolf Virchow   first proposed that all cells arise from preexisting cells in 1858  
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Transmission Electron Microscope (TEM)   -used to study the cells interior -theoretical resolving power 0.5nm -practical resolving power 2.0nm  
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Scanning Electron Microscope   -used for 3D imaging of structures -resolving power of 10nm  
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Plasma Membrane   separates each cell from its environment, creating a segregated, but not isolated compartment; consist of a phospholipid bilayer  
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Functions of the Membrane   - selectively permeable - important in communicating with adjacent cells and receiving signals - allows maintaining of homeostasis  
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Prokaryotic Cells   - can live off more different and diverse energy sources than any other living thing - can inhabit greater environment extremes - generally smaller than eukaryotic cells - single cell, sometimes found in groups  
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Eukaryotic Cells   - found in plants, animals, fungi and protists - have two things not usually found in prokaryotes: cytoskeleton and membranous compartment  
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Nucleus   stores most of the cell's DNA; usually the largest organelle in an eukaryotic cell  
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Functions of the Nucleus   1) site of DNA duplication to support cell reproduction 2) site of DNA control of cellular activities 3) nucleolus is the site of synthesis of RNA  
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Ribosome   used in prokaryotic & eukaryotic cells to synthesize proteins  
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Endoplasmic Reticulum   system of interconnected membranes branching throughout the cytoplasm ** can be found as tubes or flattened sacs  
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Rough ER   - studded with ribosomes - may be continuous with the nuclear envelope - modifies proteins - transport vesicles  
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Smooth ER   - lacks ribosomes attached to it - many different functions, often pertinent to cell type  
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The Golgi Apparatus (Golgi)   - discovered initially by Camillo Golgi in 1898 - existence not confirmed until 1950's and advent of TEM **consists of flattened sacs (cisternae) and small membrane-enclosed vesicles  
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Two Poles of Golgi   1) Cis-face (receiving) 2) Trans-face (shipping)  
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What happens in the Golgi?   modification of proteins  
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Two Organelles in Eukaryotic Cells that Process Energy   Chloroplasts and Mitochondria  
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Mitochondrion   - double membrane organelle - number per cell will vary  
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Mitochondrial Matrix   - region enclosed by inner membrane - contains the DNA and ribosomes needed to make some of the proteins used in cellular respiration  
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Mitochondrial DNA   - exists as a circular DNA molecule - attached to the inner membrane of the mitochondria - maternally inherited  
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What is energy?   the ability to do work  
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potential energy   energy which is stored or at rest  
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kinetic energy   energy in action or at work  
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Types of Energy   - Total energy (enthalpy) = H - Usable energy (free) = G - Unusable energy (entropy) = S - Absolute Temperature = T  
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1st Law of Thermodynamics   Energy is neither created nor destroyed, it only changes from one form to another; energy is conserved.  
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2nd Law of Thermodynamics   The total energy of a system always decreases and results in an increase in entropy or disorder.  
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closed energy system   system which is not exchanging energy with its surroundings  
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open energy system   system which exchanges matter and energy with its surroundings  
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spontaneous reaction   when a reaction goes to more than halfway to completion without an input of free energy -- release free energy  
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non spontaneous reaction   proceed only with an input of free energy from the environment  
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What are enzymes?   biological catalysts; speed up reactions without being consumed in the reaction  
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catalyst   molecule that facilitates a reaction without itself being consumed in the reaction  
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Coenzymes   relatively small compared with the enzyme to which they temporarily bind  
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Characteristics of Enzymes   - enzymes have an optimal temperature at which they operate most efficiently - enzymes have an optimal pH - specific in the reactions that they catalyze  
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Factors affecting enzymatic activity   - substrate concentration vs. rate of reaction - temperature vs. rate of reaction - pH vs. rate of reaction  
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turnover number   the number of molecules of substrate converted by an enzyme molecule per unit of time  
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Enzyme Inhibitors   - normal binding - competitive inhibition - noncompetitive inhibition  
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