The study of protein folding is fundamental and important in the multidisciplinary field because a diversity of diseases,like Alzheimer\'s and Parkinson\'s are relevant to protein misfolding.The current thermodynamic and geometric approaches only phenomenologically describe but do not provide a mechanistic understanding of the competition between correct folding and misfolding.Here we present a model to understand the misfolding behavior.Considering the influence of dissipative strength for all possible sequences and comparing the folding time toward different compact structures,we obtain a phase diagram of the dissipative quantum phase transition that enables us to model the behavior.We also investigate how a perturbation in the Hamiltonian affects the transition point,which motivates us to explore possible manual interventions.Our results indicate that the manual intervention may be effective for some specific sequence but not for everyone.This approach is expected to lay a foundation for further studies on manual intervention in protein misfolding.