Observation of dielectric universalities in albumin, cytochrome C and Shewanella oneidensis MR-1 extracellular matrix. Issue 1 (December 2017)

• Record Type: Journal Article
• Authors: Motovilov, K.; Savinov, M.; Zhukova, E.; Pronin, A.; Gagkaeva, Z.; Grinenko, V.; Sidoruk, K.; Voeikova, T.; Barzilovich, P.; Grebenko, A.; Lisovskii, S.; Torgashev, V.; Bednyakov, P.; Pokorný, J.; Dressel, M.; Gorshunov, B.
• Is Part Of: Scientific reports. Volume 7:Issue 1(2017)
• Page Start: 1
• Page End: 11
• Publication Date: 2017-12
• Subjects: Natural history -- Research -- Periodicals; Biology -- Research -- Periodicals; Physical sciences -- Research -- Periodicals; Earth sciences -- Research -- Periodicals; Environmental sciences -- Research -- Periodicals; 502.85
• DOI: 10.1038/s41598-017-15693-y
• Languages: English
• ISSNs: 2045-2322

Abstract

Abstract The electrodynamics of metals is well understood within the Drude conductivity model; properties of insulators and semiconductors are governed by a gap in the electronic states. But there is a great variety of disordered materials that do not fall in these categories and still respond to external field in an amazingly uniform manner. At radiofrequencies delocalized charges yield a frequency-independent conductivityσ 1 (ν ) whose magnitude exponentially decreases while cooling. With increasing frequency, dispersionless conductivity starts to reveal a power-law dependenceσ 1 (ν )∝ν s withs < 1 caused by hopping charge carriers. At low temperatures, such Universal Dielectric Response can cross over to another universal regime with nearly constant loss ε″∝σ1 /ν = const. The powerful research potential based on such universalities is widely used in condensed matter physics. Here we study the broad-band (1–1012 Hz) dielectric response ofShewanella oneidensis MR-1 extracellular matrix, cytochrome C and serum albumin. Applying concepts of condensed matter physics, we identify transport mechanisms and a number of energy, time, frequency, spatial and temperature scales in these biological objects, which can provide us with deeper insight into the protein dynamics.