论文部分内容阅读
Recent years,the green fluorescent protein(GFP)family has been extensively studied and utilized in many applications,mainly owing to their unique biochemical and optical characteristics.However,there are too many parameters such as hydrogen bond,π-π stack,van de Waals force,medium viscosity and static electronic interaction which could influence the luminous efficiency and frequency,and thereby enhance the control difficulty [1].Here we employ theoretical simulations to investigate the underlying mechanism of luminescence behavior of a GFP model molecule,and examine the effect of environment.It was revealed by our work that the proton addition and hydrogen bonding with water molecules could greatly improve the emission of green light by GFP,a property which is useful but mainly found in native biologically active environment(inside the protein).This suggests that the green light emission of GFP relies on the cage environment of protons and water molecules.Inspired by our findings,experimental work has been done and demonstrated that the artificial proton and water rich environment could indeed improve the green light emission.Following this track,one could discover novel fluorescent properties for GFP which will make sense in the application of the biomedicine,fluorescence labeling and other biochemical materials[2].