The Journal of Physical Chemistry B, Год журнала: 2025, Номер unknown

Опубликована: Фев. 20, 2025

Salts readily alter the physical properties of intrinsically disordered proteins (IDPs) rich in charged residues. Using a coarse-grained IDP model and computer simulations, we investigated how salts affect heterogeneous conformational ensemble segment-level structures prothymosin-α, classified as polyelectrolyte. We show that clusters conformations with distinct structural features are present within prothymosin-α by projecting it onto two-dimensional latent space aid autoencoders. Although is inherently disordered, there preferred transitions between these conformations. Changing salt concentration led to formation new or/and disappearance existing clusters, contributing changes properties. Shuffling Skopelitian domain (C-terminal sequence) known for its anticancer activity, resulted different cluster, indicating specific related particular function. The multiple could be correlated functions, or inhibit functions modulating population clusters.

Язык: Английский