Thermal denaturation and structural changes of α-helical proteins in keratins

• Published in: Journal of structural biology Vol. 177; no. 2; pp. 553 - 560
• Main Authors: Wortmann, Franz J., Wortmann, Gabriele, Marsh, Jennifer, Meinert, Knut
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.02.2012
• Subjects: Algorithms; Calorimetry, Differential Scanning; Collagen; Denaturation; DSC; Hair - chemistry; Hair - ultrastructure; Human hair; Humans; Keratin; Keratins - chemistry; Models, Molecular; Protein Denaturation; Protein Stability; Protein Structure, Secondary; Thermodynamics; Transition Temperature; α-Helix; Keratin; α-Helix; DSC; Human hair; Denaturation; Collagen
• ISSN: 1047-8477; 1095-8657
• DOI: 10.1016/j.jsb.2011.09.014

To gain insight into the thermal stability of intermediate filaments and matrix in the biological composite structure of α-keratins, the thermal denaturation performance of human hair fibers was investigated by Modulated Differential Scanning Calorimetry (MDSC) in the dry and the wet state. Denaturation enthalpy ΔHD in water was found to be independent of heating rate (11.5J/g) and to be approximately double as high as in the dry state (5.2J/g). The lower enthalpy (dry) and its dependency on heating rate are attributed to effects of pyrolysis. The stepwise change of reversing heat capacity ΔCp marks the denaturation process as a classic two-stage transition. The increase of ΔCp with heating rate reflects a continuous shift of the nature of the denaturation of the α-helical material, first, into random coil and then towards random β-materials for lower heating rates. Denaturation temperatures follow Arrhenius relationships with heating rate, yielding activation energies of 416kJ/mol (dry) and 263kJ/mol (wet), respectively. A decrease of activation energy (wet) for high heating rates supports the hypothesis of systematic changes of the pathway of denaturation.