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- https://bio.libretexts.org/Bookshelves/Biochemistry/Fundamentals_of_Biochemistry_(Jakubowski_and_Flatt)/01%3A_Unit_I-_Structure_and_Catalysis/01%3A_The_Foundations_of_Biochemistry/1.03%3A_Physical-Chemical_FoundationsThis page delves into the fundamentals of chemical kinetics and thermodynamics within biochemistry. It explains key concepts such as reaction rates, activation energy, reaction mechanisms, the transit...This page delves into the fundamentals of chemical kinetics and thermodynamics within biochemistry. It explains key concepts such as reaction rates, activation energy, reaction mechanisms, the transition state, and how these factors, alongside thermodynamic principles like enthalpy, entropy, and Gibbs free energy, dictate reaction spontaneity and equilibrium.
- https://bio.libretexts.org/Bookshelves/Biochemistry/Fundamentals_of_Biochemistry_(Jakubowski_and_Flatt)/02%3A_Unit_II-_Bioenergetics_and_Metabolism/12%3A_Bioenergetics_and_Biochemical_Reaction_Types/12.01%3A_Biochemical_Reactions_and_Energy_ChangesThe page outlines key learning goals for biochemistry majors, focusing on understanding free energy reaction diagrams, oxidation numbers, and the reactivity of aldehydes, ketones, and carboxylic acid ...The page outlines key learning goals for biochemistry majors, focusing on understanding free energy reaction diagrams, oxidation numbers, and the reactivity of aldehydes, ketones, and carboxylic acid derivatives. It aims to help students analyze reaction energetics, distinguish nucleophilicity from basicity, and apply these concepts to metabolic and enzymatic processes.
- https://bio.libretexts.org/Bookshelves/Biochemistry/Fundamentals_of_Biochemistry_(Jakubowski_and_Flatt)/01%3A_Unit_I-_Structure_and_Catalysis/04%3A_The_Three-Dimensional_Structure_of_Proteins/4.08%3A_Protein_Folding_and_Unfolding_(Denaturation)_-_DynamicsThis page provides a comprehensive overview of protein folding, detailing the processes involved, such as thermodynamics driving Gibbs free energy changes, kinetics of folding pathways, and the transi...This page provides a comprehensive overview of protein folding, detailing the processes involved, such as thermodynamics driving Gibbs free energy changes, kinetics of folding pathways, and the transition between native, intermediate, and denatured states. It discusses factors influencing protein denaturation, including temperature and chemical denaturants, and the role of molecular chaperones in assisting folding.
- https://bio.libretexts.org/Bookshelves/Biochemistry/Fundamentals_of_Biochemistry_(Jakubowski_and_Flatt)/01%3A_Unit_I-_Structure_and_Catalysis/04%3A_The_Three-Dimensional_Structure_of_Proteins/4.09%3A_Protein_Stability_-_ThermodynamicsThe page delves into protein stability, discussing the balance between folding and unfolding dynamics influenced by thermodynamic factors. Key forces like hydrogen bonds, ion pairs, van der Waals forc...The page delves into protein stability, discussing the balance between folding and unfolding dynamics influenced by thermodynamic factors. Key forces like hydrogen bonds, ion pairs, van der Waals forces, and the hydrophobic effect affect protein stability. It highlights experimental approaches, such as site-directed mutagenesis, to study these forces. Environmental factors, such as pH and temperature, also influence protein behavior.
- https://bio.libretexts.org/Courses/Roosevelt_University/BCHM_355_455_Biochemistry_(Roosevelt_University)/06%3A_Enzyme_Thermodynamics/6.05%3A_ThermodynamicsEnergy in biological systems follows the laws of thermodynamics. The First Law states that energy is conserved and transferred, while the Second Law introduces entropy, which always increases, making ...Energy in biological systems follows the laws of thermodynamics. The First Law states that energy is conserved and transferred, while the Second Law introduces entropy, which always increases, making energy less available for work. Although local decreases in entropy can occur, the universe’s total entropy must always rise.
