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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/4.07%3A_Fibrillar_ProteinsThe page discusses various fibrillar proteins, focusing on their structure, function, and role in biological systems. It describes different types of fibrillar proteins, such as collagen, ??-keratin, ...The page discusses various fibrillar proteins, focusing on their structure, function, and role in biological systems. It describes different types of fibrillar proteins, such as collagen, ??-keratin, elastin, and fibrinogen, and highlights their structural characteristics, including unique amino acid compositions and hierarchical organizations.
- 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/4.02%3A_Secondary_Structure_and_LoopsThe page provides a detailed exploration of secondary structures in proteins, focusing on alpha helices, beta sheets (parallel and antiparallel), 310 helices, pi helices, and loops and turns. It expla...The page provides a detailed exploration of secondary structures in proteins, focusing on alpha helices, beta sheets (parallel and antiparallel), 310 helices, pi helices, and loops and turns. It explains the roles of hydrogen bonds in stabilizing structures and discusses sequence determinants that influence structural propensities. The text also covers the characteristics and roles of loops, turns, and linkers, and examines amino acid propensities for forming different secondary structures.
- https://bio.libretexts.org/Under_Construction/OLI/Biochemistry/Unit_2%3A_Biochemistry/Module_4%3A_Protein_Structure/Module_4.4%3A_Tertiary_Structure_and_Protein_StabilityProtein unfolding involves the conversion of the highly ordered native state (folded) state to a unfolded (denatured) state. During the unfolding process the primary structure (e.g. covalent bonds) of...Protein unfolding involves the conversion of the highly ordered native state (folded) state to a unfolded (denatured) state. During the unfolding process the primary structure (e.g. covalent bonds) of the protein does not change. The folded state usually has a single, well defined, and unique tertiary structure with a significant fraction of amino acids buried in the core of the protein, sequestered from the solvent. All amino acid sidechains will be exposed to the solvent in the unfolded state.
- https://bio.libretexts.org/Bookshelves/Biochemistry/Fundamentals_of_Biochemistry_(Jakubowski_and_Flatt)/Unit_IV_-_Special_Topics/32%3A_Biochemistry_and_Climate_Change/32.12%3A__Part_3_-_A_Warmer_World%3A_Temperature_Effects_On_ProteinsThis page covers various learning goals related to biochemistry, particularly focusing on protein thermal stability, denaturation mechanisms, heat-shock responses, adaptations in thermophiles, enzyme ...This page covers various learning goals related to biochemistry, particularly focusing on protein thermal stability, denaturation mechanisms, heat-shock responses, adaptations in thermophiles, enzyme kinetics, and experimental methods for studying thermal effects. It emphasizes the biological importance of these concepts in the context of climate change and their applications in biotechnology and pharmaceuticals.
- 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/2.04%3A_Solubility_in_an_aqueous_world_-_noncovalent_interactions_in_depthThe page provides an in-depth exploration of noncovalent interactions within biochemistry, touching on hydrogen bonding, ionic interactions, van der Waals forces, and more. It connects these interacti...The page provides an in-depth exploration of noncovalent interactions within biochemistry, touching on hydrogen bonding, ionic interactions, van der Waals forces, and more. It connects these interactions to water???s properties, explaining how they influence solubility and biological structures such as protein folding.
- 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/2.02%3A_Weak_Acids_and_Bases_pH_and_pKaThis page discusses fundamental concepts of biochemistry, focusing on acids, bases, and pKa. It outlines the properties and significance of strong and weak acids and bases in biochemical contexts and ...This page discusses fundamental concepts of biochemistry, focusing on acids, bases, and pKa. It outlines the properties and significance of strong and weak acids and bases in biochemical contexts and introduces the concept of pKa to describe acid strength. The page also explains the application of the Henderson-Hasselbalch equation for calculating pH and discusses titration curves, buffering regions, and the prediction of protonation states in biochemical systems.
- 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/4.03%3A_Tertiary_and_Quaternary_StructuresThe page discusses the fundamentals of biochemistry with a focus on tertiary and quaternary protein structures. Learning goals include distinguishing between tertiary and quaternary protein structures...The page discusses the fundamentals of biochemistry with a focus on tertiary and quaternary protein structures. Learning goals include distinguishing between tertiary and quaternary protein structures, understanding forces stabilizing tertiary structures, identifying domains and motifs, and exploring protein folding pathways. It also covers analyzing oligomerization, allosteric regulation, structural organization, interpreting structural data, and the impact of mutations on protein structures.
- 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/4.06%3A_Intrinsically_Disordered_ProteinsThis page provides a comprehensive overview of Intrinsically Disordered Proteins (IDPs), detailing their characteristics, biological roles, structural dynamics, and relevance in health and disease. ID...This page provides a comprehensive overview of Intrinsically Disordered Proteins (IDPs), detailing their characteristics, biological roles, structural dynamics, and relevance in health and disease. IDPs are unique as they lack fixed three-dimensional structures but are involved in crucial cellular functions like molecular recognition and signaling. The page covers the experimental methods for identifying IDPs, evolutionary perspectives, and implications in disease and therapeutics.
- 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/4.05%3A_Protein_with_Alpha_Alpha-Beta_Beta_and_Little_Secondary_StructureThe page outlines learning goals related to understanding protein structure, emphasizing the classification of proteins based on their secondary structure. It guides students to distinguish between ma...The page outlines learning goals related to understanding protein structure, emphasizing the classification of proteins based on their secondary structure. It guides students to distinguish between major classes of protein folds, examining the role of ??-helices, ??-sheets, and disordered regions in shaping protein topology and function.
- 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.
