Osmolyte-Programmed Bio-fabrication: Tailoring the Macroscopic Architecture of Lysozyme Hydrogels

This repository contains raw and processed experimental data documenting the heat-induced gelation and aggregation of lysozyme in the presence of Trimethylamine N-oxide (TMAO) and urea. The dataset is structured chronologically across five distinct folders to reflect the step-by-step methodology of the study: 1. Initial Screening: Mapping the gelation boundary across a broad concentration matrix using photographic records, Excel data sheets, and Fourier-transform infrared spectroscopy (FTIR) spectra of lyophilized samples.2. Optimized Matrix Screening: Systematic phase behavior tracking of a 5x5 concentration matrix under a fixed, optimized 15-minute thermal treatment duration.3. Kinetic Study: Time-series analysis (5 to 30 minutes) capturing the specific aggregation kinetics along the diagonal of the concentration matrix.4. Urea Effect: Quantitative evaluation and photographic monitoring of chemical perturbation induced by adding varying molar ratios of urea into pre-optimized baseline systems, including key reference controls.5. SEM Images: High-resolution Scanning Electron Microscopy micrographs providing a detailed look into the network morphology, categorized into control samples, binary (TMAO-protein) mixtures, and ternary (TMAO-urea-protein) mixtures. All folders contain detailed, individual Description.txt files clarifying the specific file-naming conventions, concentration index keys, and optical imaging parameters (standard vs. bottom-up illumination) utilized throughout the project.