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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)/01%3A_Unit_I-_Structure_and_Catalysis/02%3A_Water_and_its_Role_in_Life/2.05%3A_Solubility_in_an_aqueous_world_-_The_Hydrophobic_EffectThe page explores the hydrophobic effect and its significance in biochemistry. It begins with defining the hydrophobic effect, emphasizing entropy and hydrogen-bonding networks. It discusses enthalpic...The page explores the hydrophobic effect and its significance in biochemistry. It begins with defining the hydrophobic effect, emphasizing entropy and hydrogen-bonding networks. It discusses enthalpic and entropic contributions to molecular aggregation in water, highlighting ordered water structures. The page links the hydrophobic effect to protein folding, membrane formation, enzyme sites, and biomolecular organization.
- 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.
