Influence of glycerol on the structure and thermal stability of lysozyme: a dynamic light scattering and circular dichroism study.
Photon correlation spectroscopy and circular dichroism have been used to study the role of hydration in the structure and thermostability of the model protein lysozyme in water-glycerol mixtures. Two cases have been considered: water-rich and glycerol-rich regimes of concentrations. We follow the thermal denaturation both by optical spectral changes and hydrodynamic radius variations. This methodology allows us to emphasize the relevant role played by hydrophobic interactions during the process in aqueous solutions and, in glycerol, to distinguish the non-cooperative melting of secondary structure, supporting the view of a protein transition to a molten globule-like state.
Esposito
Alessandro
A
Dipartimento di Fisica, Università di Perugia, Via Pascoli, I-06123 Perugia, Italy.
Comez
Lucia
L
Cinelli
Stefania
S
Scarponi
Filippo
F
Onori
Giuseppe
G
D002942:Circular Dichroism; D005990:Glycerol / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry*; D055550:Protein Stability; D017433:Protein Structure, Secondary; D013696:Temperature
D009113:Muramidase; D005990:Glycerol