Transcription factors and chaperone proteins play a role in launching a faster response to heat stress and aggregation

Proteins, under conditions of cellular stress, typically tend to unfold and form lethal aggregates leading neurological diseases like Parkinson's Alzheimer's. A clear understanding the that favor dis-aggregation restore cell its healthy state after they have been stressed is therefore important in dealing with these diseases. The heat shock response (HSR) mechanism a signaling network deals undue protein aids maintenance homeostasis within cell. This framework, on own, mathematically well studied mechanism. However, not much known about how various intermediate mis-folded states aggregation process interact some key components HSR pathway such as Heat Shock Protein (HSP), Transcription Factor (HSF) HSP-HSF complex. In this article, using kinetic parameters from literature, we propose analyze two mathematical models for also include explicit reactions formation aggregates. Deterministic analysis stochastic simulations show folded proteins misfolded exhibit bistability certain region parameter space. Further, highlight role HSF HSF-HSP complex reducing time lag stress re-folding all back their native state. These models, therefore, call attention significance studying related pathways conjunction each other.