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Gen Biology Exam 3

Ch. 4,5,6

QuestionAnswer
made flattened sacs called cisternae. continuous with outer membrane of nuclear envelope. Rough Endoplasmic Reticulum
Tubules (structure), NO ribosomes attached, and biological membrane. Smooth Endoplasmic Reticulum
1)ER and outer membrane of the nuclear envelope 2)Golgi apparatus 3)lysosomes 4)various vacuoles (storage site) and vesicles (shuttles) 5)plasma membrane Endomembrane system
makes up at least half of all the membrane Endoplasmic Reticulum
lipids, carbohydrates, and proteins Biosynthetic Factory (ER)
1)lipid biosynthesis (oils, phospholipids, steroids) 2)metabolism of carbohydrates 3)detoxification of drugs and poisons Smooth ER functions
Most secreted and membrane boud proteins made in the ER. Folded and modifidied in the lumen of the ER. Rough ER functions
1)glycosylation 2)phosphorylation-S,Y,T amino acids Types of modification in the Rough ER
Protein that is glycosylated in the Rough ER Glycoproteins
shipping and receiving center of the cell -products of the ER modified further and stored or shipped -cisternal maturation model Golgi apparatus
Recycling center. -membrane bound organelle that is filled with hydrolytic enzymes Lysosome
Disease in the lysosome Tay sacks
Plays a role in renewing cellular components Autophagy (in the Lysosome)
Plant cells: maintenance compartments Large vacuoles
-food vacuole -contractile vacuole (water balance) Types of Large Vacuoles
large membrane-bound structure. Part of the plant's EMS Central Vacuole
Structure is Surrounded by the tonoplast,Forms by fusion of vesicles, and Unique solution Structure for Central Vacuole
-storage for pigments and poisons -storage for ions. K+, Cl- -disposal site -storage for organic compounds Types of Functions for Central Vacuole
Convert energy into forms a cell can use - they have DNA, chromosomes are circular -Ribosomes Mitochondria and Chloroplast
is the site of cellular respiration. ATP energy Mitochondria
is the site of photosynthesis Chloroplast
Both have more than one membrane -2 membranes. outer is smooth. inner is folding. -3 membranes Mitochondria and Chloroplast
Oxidation site Peroxisome
Reduction-oxidation Redox reactions
specialized compartment for carrying out Redox Reactions on oxygen Peroxisome
structural support and highway system Cytoskeleton
3 types of fibers: 1) microtubules (biggest) dynamic 2)intermediate filaments (permanent) 3)microfilaments (dynamic) Cytoskeleton fibers
1) mechanical support a)help maintain cell shape b)help fix structures in place 2)motility a)intracellular movements (vessicle) b)cellular movements (cilia and flagella) 3)regulation of biochemical properties Rules of Cytoskeleton
a)found in the Cytoplasm b)hollow rod >thickest in diameter c)made of Tubuln Microtubules
Functions: 1. Maintain cell shape 2. cell motility ucilia and flagella 3. chromosome movement 4. organelle movement Microtubules
(9-3) organization, 9 triplets of microtubules. Structurally iddentical to a centriole; anchors the flagella in the cell. Basal body (of the microtubules)
smallest in diameter, made of actin, and solid rods consisting 2 intertwinded strands of actin polymers microfilaments
Functions: a) maintain cell shape b)change cell shape c) muscle contraction d) cytoplasmic streaming e)cell motility (pseudopodia) f)cell division (cell clequage function) Microfilaments
static 1)maintain cell shape 2)anchor organelles (nucleus in place) 3) nucleur lamina (maintain nucleus cell shape; keratins: nails and hair, strong fibers) 4)cell to cell connections: intercellular junctions (plants plasmodesmatas) Intermediate Filaments
3 types in animals (intercellular junctions) -neighboring cells have a strong seal between the cells tight junctions
3 types in animals (intercellular junctions) -"anchoring junctions" -fasten cells together into sheets -keratin is an important protein in the desmosome Desmosomes
3 types in animals (intercellular junctions) -a cytoplasmic channel made of membrane proteins -allows for sharing between cells -ions, sugars Gap junctions: communicating junction
syntesized by the cell and then secreted, delivered by the endomembrane system Extracellular matrix
very strong and composed of Cellulose and other Sugars Cell wall of a plant cell
organization: 1)primary cell wall- thin and flexible laid down first 2)middle lamella- thin layer (pectins) between a neighboring cells 3)secondary cell wall- laid down in thick strong layers Cell wall of a plant cell
main part: glycoproteins -collagen -fibronectin -integrins -proteoglycans animal cells
glycoproteins; most abundant collagen
glycoprotein; attaches to membrane bound proteins (integrins) fibronectin
proteins that span plasma membrane, connect inside and outside environments integrins
more sugars than protein proteoglycans
1)phospholipids- main, amphipathic 2)proteins- properties 3)carbohydrates- indentification tags 4)cholesterol- temperature buffer Biological membrane
fluidity of the biological membrane: two faces of a biological membrane- topography The fluid mosaic model
a protein in the biological membrane: penetrates the hydrophobic core of the membrane integral protein
a protein in the biological membrane: not embedded; but associate with embedded components peripheral protein
1)transport- carriers and channels 2)enzymatic activity 3)signal transduction- messenger and receptor, message from outside to inside 4)cell to cell recognition- glycoproteins 5)intercellular joining 6)attachment to the EMC or cytoskeleton Membrane protein functions
helps move things in or out of th cell - channels and carriers transport proteins
provide hydrophilic passage across membrane Channels
have shape changes when binding cargo Carriers
no energy used to mke a substance Passive transport
things move from high concentration to low concentration, (passive transport) motion of molecules Diffusion
energy is used (ATP)to move a substance against a concentration gradient Active transport
carrier or channel. protein assisted transport. (active transport) Facilitated Diffusion
diffusion of a SOLVENT across a selectively (H2O) membrane. Movement of H2O from where solutes less concentrated to where solutes are more concentrated. (passive transport) Osmosis
diffusion of a SOLUTE across the selective membrane Dialysis
ability of a solution to cause a cell to gain or lose H2O Tonicity
-SAME solutes in a solution and cell -LESS solutes " " " -MORE solutes " " " -Isotonic -Hypotonic -Hypertonic
movement of chaged and/or large molecules down their concentration gradient facilitated diffusion
pressure from the cell wall. cell rigid. turgor pressure
turgid or firm plant cell hypotonic
flaccid (limp) isotonic
plasmolysis- pulling away of membrane from the ceell wall hypertonic
provides a passage way across the membrane : aquaporin, and ion channels (gated) channels (f.d.)
undergo shape change to move cargo; specific carriers
sodium out and potassium in. ATP needed sodium-potassium pump
electical charge across the plasma membrane membrane potential (s.p.p.)
for ions, movement from more to less concentration chemical gradient
for ions, electrochemical gradient electrical gradient
movement of 2 substances at the same time Co-transport
transport 2 molecules in the same direction symporters
transport 2 molecules in opposite directions antiporters
formation of vesicles to move things in or out of the cell Bulk transport
movemement out of the cell exocytosis (B.T.)
phagocytosis, pinocytosis, and receptor-mediated Endocytosis
cellular eating. cell taken in is particulate phagocytosis
cellular drinking. liquid is taken in. common among animal cels pinocytosis
specific shape in receptor. molecules transported into eukaryotic cells receptor-mediated endocytosis
total chemical processes of a cell metabolism
breakdown reactions catabolic
build up reactions anabolic
organizational units of metabolism- the elements an organism controls to achieve coherent metabolic activity Biochemical pathways
study of how an organism uses its energy resources Bioenergetics
the capacity to do work or cause change energy
the branch if chemistry concerned with energy changes Thermodynamics
stored energy potential energy
energy of motion kinetic energy
energy can be transferred or transformed; but not created or destroyed First Law of Thermodynamics
With every energy transformation, disorder of the universe increases (entropy) Second Law of Thermodynamics
the matter under study: everything else in the universe: no energy or matter exchange between system and surroundings: Opposite of closed: -System -Surroundings -Closed system -open system
quantitative measure of disorder. S symbol Entropy
a measure of the portion of a system's energy that can perform work. Free energy
equal to the energy contained in a molecule's chemical bonds Gibbs free energy
total amount of energy (H) enthalpy
gve up total energy (-H), increase disorder (+S), both For a reaction to be spontaneous (-G)
increase total energy, decrease disorder, both For a reaction to be non-spontaneous (+G)
gives off energy, -G, spontaneous, decrease in free energy Exergonic Reaction
energy input, +G, non-spontaneous, increase in free energy (G) Endergonic Reaction
the extra energy needed to desstabilize existing chemical bonds and initiate a chemical reaction. enzymes lower this. activation energy
the process of influencing chemicl bonds in a way that lowers the activation energy needed to initiate a reaction catalysis
powers almost every energy-requiring process in cells. 3 phosphates, ribose sugar, nitrogenous base. Adenosine Triphosphate (ATP)
breakdown of ATP(exergonic)is used to drive endergonic reactions Energy Coupling
proteins that are biological _______: speeds u reactions but is not consumed (lowers activation enery) Enzymes: Catalyst
1) cannot change G of a reaction. 2)can't make an endergonic reaction exergonic. 3)can speed up reaction. 4)very selective- shape of enzyme What Enzymes do
the reactant(s) an ezyme acts on substrate
region on the surface that binds to a substrate active site of the enzyme
compatability between active site and substrate specifity of the enzyme
occurs when the chemical groups of a substrate interact with the amino acids of the active site (shape change, allusteric change) Induced fit
1)substrate enters active site of enzyme (induced fit). 2)substrate held in place by weak interactions 3)active site lower Ea by one or more of the following. 4)substrated converted to product. 5)product released... ENZYME CYCLE
1)temperature. 2)pH-7. 3)concentration. 4)cofactors- non-protein helpers of an enzyme (vitamins), coenzymes. 5)inhibitors Things that effect enzyme activity
1)Reversible- weak binding of inhibitor a)Competitive- binds to active site. b)non-competitive- binds somewhere else to cause enzyme to change shape. 2)Irreversible- covalent attachment Two types of inhibitors (effect enzyme activity)
Created by: n00688846
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