Protein Folding Mechanisms §

Group: 4 #group-4

Relations §

• Hydrogen Bonding: Hydrogen bonding between polar groups in the protein backbone and side chains contributes to the stability of the folded structure.
• Kinetics: The kinetics of protein folding, including the rates of folding and unfolding, as well as the formation of intermediates, are important in understanding the folding process.
• Disulfide Bridges: Disulfide bridges formed between cysteine residues can stabilize the folded structure of proteins, especially in extracellular proteins.
• Hydrophobic Interactions: Hydrophobic interactions are a major driving force in protein folding, where non-polar amino acid residues tend to cluster together in the core of the protein to minimize exposure to water.
• Chaperones: Chaperone proteins assist in the proper folding of other proteins, preventing misfolding and aggregation.
• Thermodynamics: The folding of proteins is driven by the thermodynamic principle of minimizing the free energy of the system, where the native folded state is typically the most stable conformation.
• Protein Folding Landscapes: Protein folding landscapes provide insights into the mechanisms by which proteins fold into their native structures.
• Ionic Interactions: Ionic interactions between charged amino acid side chains can contribute to the folding and stability of proteins.
• Van der Waals Forces: Van der Waals forces, which are weak attractive forces between atoms, also play a role in stabilizing the folded structure of proteins.
• Protein Misfolding: Misfolding of proteins can lead to the formation of insoluble aggregates, which are associated with various diseases.