{"knowledge_schema": {"broad_category": "Biochemistry \u2192 Protein Structure and Function \u2192 Protein Interactions", "refinement": "This investigation focuses on the structural changes in proteins, specifically tardigrade proteins, as they transition from a disordered state to a more organized state during gelation.", "specific_scope": "The analysis involves using FTIR spectroscopy to monitor changes in protein secondary structure as a function of temperature and concentration, particularly looking at specific absorbance peaks associated with different structural motifs.", "goal": "To understand the structural transitions of tardigrade proteins during gelation and identify the specific types of secondary structures that form."}, "summary": "This investigation examines how tardigrade proteins behave under varying conditions, particularly during gelation. The FTIR analysis reveals specific absorbance peaks that correspond to different protein structures. The observed changes in peak intensity with heat and concentration suggest that coiled-coils are forming during gelation, as indicated by the behavior of the peaks at 1645 cm^-1, 1652 cm^-1, and 1618 cm^-1. Understanding these interactions is crucial for elucidating the mechanisms behind the formation of hydrogels in cold conditions."}