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- 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/Bookshelves/Biochemistry/Fundamentals_of_Biochemistry_(Jakubowski_and_Flatt)/01%3A_Unit_I-_Structure_and_Catalysis/04%3A_The_Three-Dimensional_Structure_of_Proteins/4.04%3A_Secondary_Structural_Motifs_and_DomainsThe page provides a comprehensive overview of structural motifs and domains in proteins, aimed at biochemistry majors. It covers the differentiation between motifs and domains, recognizing common stru...The page provides a comprehensive overview of structural motifs and domains in proteins, aimed at biochemistry majors. It covers the differentiation between motifs and domains, recognizing common structural motifs, exploring their evolutionary significance, and the experimental and computational methods to analyze them. The page also discusses protein architecture, with examples like the TIM barrel, Rossmann fold, and beta-propellers.
- 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/4.12%3A_Laboratory_Determination_of_the_Thermodynamic_Parameters_for_Protein_DenaturationThe page offers a detailed exploration of protein denaturation, highlighting the key thermodynamic parameters such as ΔG, ΔH, and ΔS that are central to understanding protein stability. It covers expe...The page offers a detailed exploration of protein denaturation, highlighting the key thermodynamic parameters such as ΔG, ΔH, and ΔS that are central to understanding protein stability. It covers experimental techniques like UV and fluorescence for measuring denaturation, and describes how to interpret denaturation curves to calculate the standard free energy of unfolding.
