  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.
