.png){kind=icon}
返回
Enzyme leaps fuel antichemotaxis
.png){kind=icon}
OA
AI
DOI：10.1073/pnas.1717844115.png)
.png){kind=icon}
.png){kind=icon}
分享.png){kind=icon}
收藏
摘要
En 中文
There is mounting evidence that enzyme diffusivity is enhanced when the enzyme is catalytically active. Here, using superresolution microscopy [stimulated emission-depletion fluorescence correlation spectroscopy (STED-FCS)], we show that active enzymes migrate spontaneously in the direction of lower substrate concentration (antichemotaxis) by a process analogous to the run-and- tumble foraging strategy of swimming microorganisms and our theory quantifies the mechanism. The two enzymes studied, urease and acetylcholinesterase, display two families of transit times through subdiffraction-sized focus spots, a diffusive mode and a ballistic mode, and the latter transit time is close to the inverse rate of catalytic turnover. This biochemical information-processing algorithm may be useful to design synthetic self-propelled swimmers and nanoparticles relevant to active materials. Executed by molecules lacking the decision-making circuitry of microorganisms, antichemotaxis by this run-and-tumble process offers the biological function to homogenize product concentration, which could be significant in situations when the reactant concentration varies from spot to spot.
Keyword:
enzyme
chemotaxis
active matter
FCS
fluorescence correlation spectroscopy
AI总结
对已上传原文的论文进行重点信息的提取，主要内容包括：简要概述、研究摘要、背景介绍、关键亮点、图文解析、展望与总结。
期刊
P
IF:
9.1
论文数:
10.8W
被引数:
73.5W
机构
引用论文
.png){kind=icon}
Spectral Reflectance Characteristics of Laboratory-Grown Salt Crusts on Silty Clay and Sandy Soils
PREAI
分享收藏分享收藏
查看更多内容