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- https://bio.libretexts.org/Bookshelves/Biochemistry/Fundamentals_of_Biochemistry_(Jakubowski_and_Flatt)/01%3A_Unit_I-_Structure_and_Catalysis/10%3A_Lipids/10.02%3A_Lipids_Aggregates_in_Water_-_Micelles_and_LiposomesThe page provides a detailed overview of the structural and biochemical properties of lipids, focusing on single and double-chain amphiphiles, micelles, and bilayers. It explains how amphiphiles aggre...The page provides a detailed overview of the structural and biochemical properties of lipids, focusing on single and double-chain amphiphiles, micelles, and bilayers. It explains how amphiphiles aggregate in water, forming structures like micelles and liposomes, driven by thermodynamics and noncovalent interactions. The page delves into the critical micelle concentration (CMC), the hydrophobic effect, and the role of noncovalent forces.
- 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.
