{
    "knowledge_schema": {
        "broad_category": "Biochemistry \u2192 Protein Structure and Interactions \u2192 Protein Folding and Gelation",
        "refinement": "This problem focuses on the behavior of tardigrade proteins during gelation, specifically how their secondary structures change in response to concentration and temperature.",
        "specific_scope": "The investigation involves analyzing FTIR spectra to understand the structural transitions of proteins as they form hydrogels upon hydration and heating.",
        "goal": "Identify the correct explanation for the observed FTIR spectral changes in relation to protein structure transitions during gelation."
    },
    "summary": "The problem involves studying the structural changes of tardigrade proteins as they form cold setting hydrogels. The FTIR spectra show specific peaks that indicate different secondary structures, and their behavior changes with concentration and heating. The goal is to determine the correct explanation for these spectral changes, focusing on how disordered structures transition into ordered forms, such as alpha helices or beta sheets, during the gelation process. The observed dual increase in peaks at 1652 cm^-1 and 1618 cm^-1 with concentration suggests that disordered structures are folding into both alpha helices and beta sheets upon gelation."
}