Thermal signatures of biomolecules: an effective tool for screening biological defects

Abstract

We investigate the impact of environmental factors and biological defects on the thermal properties of single-helical proteins by analyzing their electronic specific heat (ESH) at constant volume (\(C_v\)). To accurately model these biomolecules, we consider their helical structure and long-range electron hopping within a tight-binding framework. Our findings demonstrate that the ESH spectra can differentiate between defective and pure helical protein molecules, even a sample with a very low contamination (single site defect) level. By comparing the ESH spectra of perfect and defective proteins, we can identify the relative location of the defect and distinguish them based on the level of contamination. This approach could be valuable for medical diagnosis of biological defects and serve as a preliminary screening method before resorting to whole genome sequencing, thereby saving time and resources.

Schematic view of a single helical protein molecule. The solid black dots along the helix (green curve) represent the amino acid residues. The dotted black lines between adjacent residues indicate the respective hopping amplitudes (t1 - t6)