Abstract
Internal molecular equilibrium fluctuations have been studied for α-amylase in two different types of samples. The comparison of incoherent neutron scattering from the enzyme in hydrated powders and in solutions gives insights into the protein - solvent interaction. Although the protein is already fully hydrated at h = 0.4 in a powder sample (the protein surface is completely covered with solvent), the proteins are characterised by a significantly larger structural flexibility in solution as compared proteins in powder samples. As obtained from model fits describing local diffusion, the results indicate that the higher mobility of solvent molecules in solution initiate additional fluctuations in the protein structure. Due to much more solvent surrounding the protein in solutions, the picosecond fluctuations of the enzyme seem to be damped, indicated by smaller amplitudes and a weaker temperature dependence as compared to powder samples.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
