Chapters 3, 4, 11, 12 Cellular Biology
Chapters 3, 4, 11, 12 Cellular Biology Bio 300
Virginia Commonwealth University
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This 5 page Bundle was uploaded by Jewelle Williams on Sunday July 24, 2016. The Bundle belongs to Bio 300 at Virginia Commonwealth University taught by Dr Teshelle A. Ponteen Green in Summer 2016. Since its upload, it has received 21 views. For similar materials see Cellular and Molecular Biology in Biology at Virginia Commonwealth University.
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Date Created: 07/24/16
Test 2 Summary Chapters 3,4,11,12 Chapter 3 Energy, Catalysis, and Biosynthesis and 4 The shape and structure of Protien: Photosynthesis: o Stage 1 converts energy from captured sunlight and stroes it as energy in chemical bonds using All of the O2 we breathe is from the splitting of water molecules st in the 1 stage o Stage 2 uses activated carriers to transport the stored energy Photosynthesis and Cellular respiration are complementary processes meaning they can go both ways Respiration: o Energy is exstracted from food molecules by oxidation (controlled burning) it is a step by step process that allows the most work for a given amount of energy o Oxidaiton is the addition of O2 to a molecule. (often its when electrons are transferred Oxidation/reduction) o Hydrogenation is reduction, Dehydrogenation is oxidation Chemical Reacitons: o They proced in the direction that protduces a loss in free energy (- change in G) The spontaneous reaction of a chemical reaction is “downhill” o Activation energy is the boost that states the “downhill” reaction Enxymes Lower the activation energy alloing these processe to happen Catalysts (molecules that increase the rate of a chemical reaction) are required for metabolism o Anabolism: the process of building large moleules (like protines) from small subunits (like amino acids) o Catabolism Breaking down large molecules into large subunits Enzymes are catalysts that lower the activation energy without changing the total change in G First Law of Thermodynamics- Energy can not be cereated or destroyed it can only change forms Second Law of Thermodynamics- The amount of entropy is always increasing o Heat is the most disordered form of energy o Disorder increases when useful energy that could be used to do work is dissipated to heat All react ions must waste more energy than they produce They are highly specific and selective Coupling reactions couple an expthermic reaction of greater magnitude with an endothermic reaction of smaller magnitude to preserve as much energy as possible in a given reaction pair o Free-Energy: Useful energy in a system is call gree enrgy (delta G) ENergeticalt favorable reactions decrease the amount of usefil energy in a system (negative delta G) Energetically Unfavorable reactions produce a positive delta G These types of reactions only occur when they are coupled with an energetically favorable reaction (negative delta G) with an energetically unfavorable reation For reactions at chemical equilibrium no work will be done Standard Free-energy Measurements: o 1 mole/lieter for molecules ∆G=∆G°+RTln [X] o Kilocalories/mole for delta G: [ ] Avagadros constant (K): 6×10 23 ℃ Normal Temperature is 37 RT at normal temperature is: 0.616 X ] K= o K is the equilibrium constant [ ] . K becomes lrger as the binding energy increases and vice versa The direction of a rea tion depends entirely on the intrinsic properties of the molecules aka: ∆ Gisdirectly porportional¿K Molecules bind together when the free-energy (usable energy) change is negative (lower than when they are separate) Random thermal motion (diffusion/osmosis) allows substrates to find the correct enzyme. Binding and catalysis takes a fraction of a second to complete. The time it takes for binding of a substrate and release of a product to occur is called the turnover number Michaelis Constant ( K m ) is the concentration of substrat at which the enzyme works at half of its mazimum speed o Small K m means strong binding to the enxyme. Conversly a large K m means a weak binding to the enzyme o Vmax 1 V 2 max Activated Carriers K m o Small inorganic molecules that contain one or more energy rich covalent bonds (ex: ATP, NAD, NADH) ATP is the most important and versatile activated carrier. Its energy si synthesized via a engergetically favorable phosphorylation reaction Ex of Phophysorylation: Condensation reactuions Acivated carriers are usually generated in reactions coupled ti ATP hydropysis NAD+/NADH and NADP+/NADPH Carry energy I nthe fomr of 2 high energy electrons pluss a proton the energy is provided by giving up a hydride ion making the molecule more stable overall They play different roles in the cells due to their different conformations (different target molecules) Inside the cell the NAD+ to NADH is kept high while the NADP+ to NADPH ratio is kept low NAD+/NADH only helps with catabolic reactions NADP+/NADPH only helps with anabolic reacitons FADH2 carries energy the same way (in the electon bonds using hydrogen) o Activatied carriers allow coupled reactions to occur An energetically Unfavorable reactionand Releases Energy (Cu atesoilfmr) (Anabolism) Enzyme-catalyzed hydrolysis reactions are energetically favorable Chapter 4 Protiens Protiens: o Made up of amino acids held together by peptide bonds which determine their function o Components: R-groups/Side Chains- Which give the protien its unique properties Directionality due to N-terminus- the Amino terminous that darries an amino group C-terminus- a “carboxyl” terminus that carrys a free carboxyl group Flexibility due to: Polypeptide backbone- made by a “core sequence” of -N- C-C o 3-D conformations R-groups help determine the shape of the conformation They are energy favorable (use the least amount of energy possible Governed by Cham=peorne molecules/protines Intermolecular foces (non covalent bonds) secure the final 3-D Shape H2 bonds Electrostatic interactions Van der waals attractions Hydrophobic interactions
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