Water slowing down drives the occurrence of the low temperature dynamical transition in microgels.

ABSTRACT: The protein dynamical transition marks an increase in atomic mobility and the onset of anharmonic motions at a critical temperature (T _d), which is considered relevant for protein functionality. This phenomenon is ubiquitous, regardless of protein composition, structure and biological function and typically occurs at large protein content, to avoid water crystallization. Recently, a dynamical transition has also been reported in non-biological macromolecules, such as poly(N-isopropyl acrylamide) (PNIPAM) microgels, bearing many similarities to proteins. While the generality of this phenomenon is well-established, the role of water in the transition remains a subject of debate. In this study, we use atomistic molecular dynamics (MD) simulations and elastic incoheren

SUBMITTER: Tavagnacco L 

PROVIDER: S-EPMC11186305 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature