With the growing popularity of blockchains, modern chained BFT protocols combining chaining and leader rotation to obtain better efficiency and leadership democracy have received increasing interest. Although the efficiency provisions of chained BFT protocols have been thoroughly analyzed, the leadership democracy has received little attention in prior work. In this paper, we scrutinize the leadership democracy of four representative chained BFT protocols, especially under attack. To this end, we propose a unified framework with two evaluation metrics,i.e., chain quality and censorship resilience, and quantitatively analyze chosen protocols through the Markov Decision Process (MDP). With this framework, we further examine the impact of two key components,i.e., voting pattern and leader rotation, on leadership democracy. Our results indicate that leader rotation is not enough to provide the leadership democracy guarantee; an adversary could utilize the design,e.g., voting pattern, to deteriorate the leadership democracy significantly. Based on the analysis results, we propose customized countermeasures for three evaluated protocols to improve their leadership democracy with only slight protocol overhead and no change of consensus rules. We also discuss future directions toward building more democratic chained BFT protocols.

Protein structure prediction is pivotal for understanding the structure-function relationship of proteins, advancing biological research, and facilitating pharmaceutical development and experimental design. While deep learning methods and the expanded availability of experimental 3D protein structures have accelerated structure prediction, the dynamic nature of protein structures has received limited attention. This study introduces an innovative 4D diffusion model incorporating molecular dynamics (MD) simulation data to learn dynamic protein structures. Our approach is distinguished by the following components: (1) a unified diffusion model capable of generating dynamic protein structures, including both the backbone and side chains, utilizing atomic grouping and side-chain dihedral angle predictions; (2) a reference network that enhances structural consistency by integrating the latent embeddings of the initial 3D protein structures; and (3) a motion alignment module aimed at improving temporal structural coherence across multiple time steps. To our knowledge, this is the first diffusion-based model aimed at predicting protein trajectories across multiple time steps simultaneously. Validation on benchmark datasets demonstrates that our model exhibits high accuracy in predicting dynamic 3D structures of proteins containing up to 256 amino acids over 32 time steps, effectively capturing both local flexibility in stable states and significant conformational changes.