Role of amorphous/amorphous and crystal/amorphous water interfaces incold destabilization of proteins

DOI

Sugars and other polyhydroxycompounds are well-known cryo- and lyo-protectors which minimize destabilization of proteins and other biological systems during freeze-drying process. However, freeze-destabilization of proteins is commonly observed even in presence of sugars. There are several mechanisms proposed for freeze-destabilization of proteins, including different freeze-concentration effects, cold-denaturation of protein molecules , and destabilization of proteins due to interfaces between ice crystals and remaining unfrozen solution. In particular, formation of ice per se was shown to have destabilizing effect on protein molecules during freezing. However, details of such destabilizing effect of ice water interfaces have not been studied.In this proposed study, we will investigate water distribution in biologically-relevant glasses, in particular carbohydrate-sugar systems, and its impact on stability of proteins. We also will study the role of water interfaces, by creating different types of the interfaces, and monitoring changes in protein molecules interaction using small angle neutron scattering technique.

Identifier
DOI https://doi.org/10.5291/ILL-DATA.8-05-408
Metadata Access https://data.ill.fr/openaire/oai?verb=GetRecord&metadataPrefix=oai_datacite&identifier=10.5291/ILL-DATA.8-05-408
Provenance
Creator Shalaev, Evgenyi; Grillo, Isabelle; Curtis, Joseph; Cicerone, Marcus; Khodadadi, Sheila; Krueger, Susan; Cristiglio, Viviana
Publisher Institut Laue-Langevin
Publication Year 2013
Rights OpenAccess; info:eu-repo/semantics/openAccess
OpenAccess true
Representation
Resource Type Dataset
Size 113 MB
Version 1
Discipline Particles, Nuclei and Fields