<p>Quantum transport in biomolecular systems is of growing interest for the development of protein-based nanoelectronic devices. In this work, electron transport through protein chains coupled to nanowire electrodes is investigated using a three-dimensional tight-binding lattice framework. The protein is represented as a network of amino acid sites connected through backbone and hydrogen-bond mediated hopping pathways. To examine structural effects, three distinct protein conformations are considered. Transport properties are evaluated within the Landauer-Büttiker formalism, enabling calculation of transmission spectra and current-voltage characteristics under finite bias conditions. In addition to the thermal effects associated with the electrodes, temperature-dependent fluctuations in the hopping parameters are incorporated to account for conformational dynamics of the protein. The results reveal a strong dependence of electronic transport on molecular conformation, with significant variations in saturation current among the studied configurations. Increasing temperature leads to smoothing of the step-like current-voltage behavior and to suppression of transmission resonances. The analysis demonstrates that hydrogen-bond connectivity and the spatial arrangement of residues play a decisive role in determining dominant conduction pathways. These findings provide fundamental insight into charge migration in protein-based molecular junctions and highlight the potential of conformational control for designing tunable bioelectronic devices.</p>