Interfacial Dynamics and Growth Modes of β₂-Microglobulin Dimers.

ABSTRACT: Protein aggregation is a complex process, strongly dependent on environmental conditions and highly structurally heterogeneous, both at the final level of fibril structure and intermediate level of oligomerization. Since the first step in aggregation is the formation of a dimer, it is important to clarify how certain properties of the latter (e.g., stability or interface geometry) may play a role in self-association. Here, we report a simple model that represents the dimer's interfacial region by two angles and combine it with a simple computational method to investigate how modulations of the interfacial region occurring on the ns-μs time scale change the dimer's growth mode. To illustrate the proposed methodology, we consider 15 different dimer configurations of the β₂m D76N m

SUBMITTER: Oliveira NFB 

PROVIDER: S-EPMC10369489 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature