Niazi Sarfaraz K
College of Pharmacy, University of Illinois, Chicago, IL 60612, USA.
Pharmaceuticals (Basel). 2025 Jun 24;18(7):951. doi: 10.3390/ph18070951.
This review investigates the novel idea that proteins catalyze chemical reactions through conformational changes driven by energy derived from their collisions with water molecules. Recent studies have suggested that proteins in solution undergo constant deformation due to collisions with water molecules, generating potential energy that can be harnessed for catalytic functions. We detail the existing evidence supporting this idea, including how structures in proteins such as α-helices and β-sheets facilitate energy conversion, how conformational changes can affect the ways in which substrates attach, and how reactions occur. Combining information from computer-based methods-such as molecular dynamics simulations and machine learning models (e.g., AlphaFold)-we suggest a more complete model for understanding how proteins function beyond simply looking at their fixed shapes. This emerging view has implications for drug design, enzyme engineering, and our fundamental understanding of biological catalysis.
本综述探讨了一种新观点，即蛋白质通过与水分子碰撞所获得的能量驱动的构象变化来催化化学反应。最近的研究表明，溶液中的蛋白质由于与水分子的碰撞而不断变形，产生可用于催化功能的势能。我们详细阐述了支持这一观点的现有证据，包括蛋白质中的α螺旋和β折叠等结构如何促进能量转换、构象变化如何影响底物附着的方式以及反应是如何发生的。结合来自基于计算机的方法（如分子动力学模拟和机器学习模型，如AlphaFold）的信息，我们提出了一个更完整的模型，用于理解蛋白质如何发挥功能，而不仅仅是简单地观察它们的固定形状。这一新兴观点对药物设计、酶工程以及我们对生物催化的基本理解具有重要意义。
