Protein Folding

• Protein folding is done by weak interactions and can take countless pathways to reach either a folded state, or aggregate
• When a protein is folded, there will be more side chain interactions and less with H2O
• A negative enthalpy creates bonds
• Folding is spontaneous with a -dG and +dS
• Chaperones can prevent aggregation and aid in folding by preventing off-path reactions and preventing interactions between partially folded proteins.