Abstract
The water molecules surrounding proteins as a thin layer and those packaged in pockets and cavities shape and control their structure. Thermally Stimulated Depolarization Currents (TSDC) technique has been applied to investigate the hydration structure of six proteins with different structural motifs: pepsin,β-lactoglobulin,α-chymotrypsin, bovine serum albumin, human serum albumin and myoglobin, at very low hydration level (water vapor activity aw≈0.80) both in the native state and after treatment in trifluoroethanol/water mixture 80% (v/v). A combined approach based on the use of the TSDC technique, able to distinguish H2O dipoles belonging to the solvation shell in terms of their order degree and mobility, and of FTIR and CD spectroscopies has allowed us to reexamine the problem of conformational stability of macromolecules as a function of their hydration.
Highlights
It is well known that proteins exist and act in a predominantly aqueous solvent environment
The results showed large differences between the Thermally Stimulated Depolarization Currents (TSDC) spectra related to the two different protein conformations, for what concerns the number and position of the main peaks
With the aim to investigate how the molecular geometry and the hydration are related by analyzing the TSDC spectra dependence on the protein conformational structure, six proteins of different conformational types were considered in the present work: pepsin, β-lactoglobulin, α-chymotrypsin, bovine serum albumin (BSA), human serum albumin (HSA) and myoglobin
Summary
It is well known that proteins exist and act in a predominantly aqueous solvent environment. With the aim to investigate how the molecular geometry and the hydration are related by analyzing the TSDC spectra dependence on the protein conformational structure, six proteins of different conformational types were considered in the present work: pepsin, β-lactoglobulin, α-chymotrypsin (mainly-beta proteins), bovine serum albumin (BSA), human serum albumin (HSA) and myoglobin (mainly-alpha proteins). They were studied in the native form and after treatment in 2,2,2-trifluorethanol (TFE)/water mixture 80% (v/v). The TSDC analysis of conformational transitions induced in proteins by TFE was associated with CD spectroscopy and FTIR measurements in the Amide I region
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