We report the reversible melting of a natural protein complex, which is based on a process that breaks down the bonds of inter-domain interactions of the protein complex in the presence of water and heat. Synthetic protein melts have been reported earlier, but the liquid phase for macromolecules is rare in nature because the protein domain size is larger than the range of the attractive interactions such as van der walls. We studied the melting process by dynamic mechanical analysis (DMA) and Raman spectroscopy. Sequencing studies and comparative modeling showed that the protein complex is made of b-sheet domains. The DMA showed that the protein is stable at dry conditions, but starts to flow even at room temperature in wet conditions. Raman studies in wet conditions showed that number and size of the crystalline domains made of b-sheets do not decrease even at elevated temperatures. This unique property makes the melting of the protein complex reversible, which opens up applications as novel nanomaterials and surface coatings.

Protein melts: Examples from nature and applications in materials coatings

245th National Meeting (2013)

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