Amplification and detection of single molecule conformational fluctuation through a protein interaction network with bimodal distributions - Quantitative Biology > BiomoleculesReport as inadecuate




Amplification and detection of single molecule conformational fluctuation through a protein interaction network with bimodal distributions - Quantitative Biology > Biomolecules - Download this document for free, or read online. Document in PDF available to download.

Abstract: A protein undergoes conformational dynamics with multiple time scales, whichresults in fluctuating enzyme activities. Recent studies in single moleculeenzymology have observe this -age-old- dynamic disorder phenomenon directly.However, the single molecule technique has its limitation. To be able toobserve this molecular effect with real biochemical functions {\it in situ}, wepropose to couple the fluctuations in enzymatic activity to noise propagationsin small protein interaction networks such as zeroth order ultra-sensitivephosphorylation-dephosphorylation cycle. We showed that enzyme fluctuationscould indeed be amplified by orders of magnitude into fluctuations in the levelof substrate phosphorylation | a quantity widely interested in cellularbiology. Enzyme conformational fluctuations sufficiently slower than thecatalytic reaction turn over rate result in a bimodal concentrationdistribution of the phosphorylated substrate. In return, this network amplifiedsingle enzyme fluctuation can be used as a novel biochemical -reporter- formeasuring single enzyme conformational fluctuation rates.



Author: Zhanghan Wu, Vlad Elgart, Hong Qian, Jianhua Xing

Source: https://arxiv.org/







Related documents