Spectral entropy of the discrete Hasimoto effective potential exposes sub-residue geometric transitions in protein secondary structure

Characterizing the geometric boundaries of protein secondary structures is fundamental to understanding macromolecular folding. By applying the discrete Hasimoto map to translate backbone geometry into a one-dimensional discrete nonlinear Schrödinger potential $V_{\mathrm{re}}[n]$, we establish a frequency-domain framework for protein conformations. Short-time Fourier transform analysis across 320,453 residues from 1,986 non-redundant proteins defines a local spectral entropy $H_{\mathrm{spec}}$ that consistently orders structural states. Helical segments emerge as narrow-band low-entropy regimes dominated by zero-frequency components, whereas coils manifest as broadband noise. We demonstrate that boundaries separating these states exhibit step-like sharpness characteristic of a first-order-like geometric transition with a sub-residue median width of 0.145 residues. This abrupt kinematic transition provides a spatial counterpart to the cooperative Zimm--Bragg thermodynamic model of helix nucleation. The extreme spatial narrowness exposes an intrinsic limitation governed by the Gabor uncertainty principle, explaining why the pointwise integrability residual $E[n]$ acts as an effective high-pass filter for boundary detection. Guided by this limit we introduce a dual-probe approach combining the high-pass residual for local torsion discontinuities with a low-frequency energy ratio $R_{\mathrm{LF}}$ measuring the DC-dominated flatness of helical interiors. Unifying these complementary signals improves the detection area under the curve from 0.783 to 0.815. Because high-entropy broadband regions coincide with the flexible loops and hinges implicated in allostery, the spectral entropy of the Hasimoto potential may serve as a sequence-agnostic geometric proxy for mapping functional dynamics from backbone coordinates.

Source: arXiv:2602.21787v1 - http://arxiv.org/abs/2602.21787v1 PDF: https://arxiv.org/pdf/2602.21787v1 Original Link: http://arxiv.org/abs/2602.21787v1