Determining the purity of single-helical proteins from electronic specific heat measurements

TL;DR

This paper theoretically investigates the electronic specific heat of single-helical proteins using a tight-binding model, revealing how disorder affects thermal properties and proposing a method to distinguish defective proteins from pure ones.

Contribution

It introduces a comprehensive tight-binding model to analyze the electronic specific heat of helical proteins and suggests a novel screening technique for protein defects based on ESH spectra.

Findings

Specific heat variation differs at low and high temperatures with disorder.

Universal pattern in ESH variation with temperature across disorder strengths.

Potential application in protein defect screening before genome testing.

Abstract

We present a theoretical investigation of the electronic specific heat (ESH) at constant volume (Cv) of single-helical proteins modeled within the tight-binding (TB) framework. We study the effects of helical symmetry, long-range hopping, environment and biological defects on thermal properties. We employ a general TB model to incorporate all parameters relevant to the helical structure of the protein. In order to provide additional insights into our results for the ESH, we also study the electronic density of states for various disorder strengths. We observe that the variation of the specific heat with disorder is very different in low and high temperature regimes, though the variation of ESH with temperature possesses a universal pattern upon varying disorder strengths related to environmental effects. Lastly, we propose an interesting application of the ESH spectra of proteins. We show that by studying the ESH of single-helical proteins, one can distinguish a defective sample from a pure one. This observation can serve as the basis of a screening technique that can be applied prior to a whole genome testing, thereby saving valuable time & resources.