In Situ Observation of Chemically Induced Protein Denaturation at Solvated Interfaces.

ABSTRACT: Proteins unfold in chaotropic salt solutions, a process that is difficult to observe at the single protein level. The work presented here demonstrates that a liquid-based atomic force microscope and graphene liquid-cell-based scanning transmission electron microscope make it possible to observe chemically induced protein unfolding. To illustrate this capability, ferritin proteins were deposited on a graphene surface, and the concentration-dependent urea- or guanidinium-induced changes of morphology were monitored for holo-ferritin with its ferrihydrite core as well as apo-ferritin without this core. Depending on the chaotropic agent the liquid-based imaging setup captured an unexpected transformation of natively folded holo-ferritin proteins into rings after urea treatment but not after gu

SUBMITTER: Nirmalraj PN 

PROVIDER: S-EPMC10591235 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature