生物传感器
变构调节
发色团
化学
构象变化
配体(生物化学)
麦芽糖结合蛋白
荧光
氢键
蛋白质动力学
核糖开关
生物物理学
蛋白质结构
立体化学
分子
生物化学
光化学
重组DNA
酶
核糖核酸
生物
受体
物理
有机化学
量子力学
非编码RNA
融合蛋白
基因
作者
Melike Berksöz,Canan Atılgan
出处
期刊:Proteins
[Wiley]
日期:2024-04-04
被引量:3
摘要
Abstract Genetically encoded fluorescent biosensors (GEFBs) proved to be reliable tracers for many metabolites and cellular processes. In the simplest case, a fluorescent protein (FP) is genetically fused to a sensing protein which undergoes a conformational change upon ligand binding. This drives a rearrangement in the chromophore environment and changes the spectral properties of the FP. Structural determinants of successful biosensors are revealed only in hindsight when the crystal structures of both ligand‐bound and ligand‐free forms are available. This makes the development of new biosensors for desired analytes a long trial‐and‐error process. In the current study, we conducted μs‐long all atom molecular dynamics (MD) simulations of a maltose biosensor in both the apo (dark) and holo (bright) forms. We performed detailed hydrogen bond occupancy analyses to shed light on the mechanism of ligand induced conformational change in the sensor protein and its allosteric effect on the chromophore environment. We find that two strong indicators for distinguishing bright and dark states of biosensors are due to substantial changes in hydrogen bond dynamics in the system and solvent accessibility of the chromophore.
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