Determine and analyze the fundamental thermodynamic parameters governing the equilibrium transition between alpha-helical and random-coil states in polypeptide chains.
Modeled conformational transitions across synthetic and natural polypeptide chains using statistical thermodynamic frameworks.
Calculated changes in enthalpy, entropy, and free energy associated with helix initiation and elongation.
Quantified key propagation and nucleation parameters that regulate the cooperativity of helix formation.
Demonstrated that transition temperature and chain length directly determine structural stability and the sharpness of conformational switching.