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Biochemistry Study Skills Jess, Sally, Alief, Abrar, Casey
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Lecture 1: Main Topics Consensus 1.) Thermodynamics is the study of chemical reactions and energy transformations. If a certain reaction was to take place and reach a specific level, the chemical reaction must be monitored or controlled. 2.) High potential energy is unstable and likely to change, whereas low potential energy is stable and unlikely to change. OFTEN 3.) The rate of a reaction is determined by how OFTEN a reaction occurs, not how fast it occurs. 4.). The ΔG values determine the spontaneity of a reaction. Negative free energy (-ΔG) is spontaneous in the forward direction, positive free energy (+ΔG) is spontaneous in the backwards direction, and a ΔG of 0 is not spontaneous in either direction.
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Lecture 2: Main Topics Consensus 1.) Breaking bonds requires energy input, while making bonds releases energy, and the formation of stronger bonds is spontaneous. 2.) Enzymes lower the activation energy of a reaction and thus speed reactions whereas heat increases the energy of the reactants, allowing them to gain enough energy to meet the activation energy and react. 3.) Heat can increase reaction rates but it is not the ideal answer for most biological reactions because heat can denature many enzymes and other proteins involved in the reaction.
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Lecture 3: Main Topics Consensus 1.) Enzymes are catalysts that have the ability to speed up chemical reactions without harming the organism, like heat could. 2.) Enzymes can be reused because they are not altered in the reaction. 3.) Metabolism is a term that represents the sum of all reactions in an organism.
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Overall Consensus 1.) Thermodynamics is the study of chemical reactions and energy transformations. 2.) Because heat, in terms of a catalyst, can be harmful to an organism, enzymes are used as catalysts in organisms to speed reactions by lowering the activation energy. 3.) The value of ΔG (Gibbs free energy) indicates the spontaneity of the reaction, telling whether or not the reaction occurs in nature.
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Our Questions for Professor White -If an enzyme becomes denatured, but only to a small degree, could it possibly reform and continue to act as catalyst for the same specific reaction? -Is it possible to reverse the denaturization process of a protein? -How much faster is a catalyst compared to heat at speeding up reactions? -Where are the enzymes stored before being reused again? -How does making bonds delta G- make the energy of the transition state lower? -After the complete denaturation of an enzyme, are there any types of chemical reactions that can occur that may restore its function?
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