南京大学最新Nature Chemistry论文：AI从头设计超稳定蛋白

Core Insights - The article discusses the significance of hydrogen bonds in stabilizing protein structures, particularly in β-sheet layers, which allow proteins to withstand mechanical and environmental stress [3][6] - A research team led by Professor Zheng Peng from Nanjing University has developed a new computational design method for superstable proteins, utilizing AI, molecular dynamics simulations, and single-molecule force spectroscopy [4][10] Group 1: Research Findings - The research successfully designed a protein named "SuperMyo" that exhibits mechanical properties significantly superior to natural proteins, with a mechanical unfolding force exceeding 1000 piconewtons, which is over five times that of natural immunoglobulin domains [8] - The number of backbone hydrogen bonds in the designed proteins was increased from 4 to 33, maximizing the hydrogen bonding network and enabling tailored mechanical performance [6][8] - "SuperMyo" also demonstrates exceptional thermal stability, with a melting temperature exceeding 100°C, maintaining structural integrity even at extreme temperatures of 150°C [8] Group 2: Implications and Applications - The molecular-level stability of "SuperMyo" translates into macro properties, as hydrogels made from this protein can retain their structure and gel state after high-pressure sterilization at 121°C, unlike traditional protein hydrogels that denature under such conditions [8] - This research presents a scalable and efficient computational design strategy for creating robust proteins, providing a general method for rationally designing proteins that can withstand extreme environments [10]