Structural Study of the Folding of a Small β Hairpin Protein

The method by which proteins adopt their native conformation based on their amino acid sequence and the interactions with their solvent environment remains an area of active research. We aim to understand the intramolecular residue-residue interactions and residue-solvent interactions involved in the formation of a β hairpin by studying the thermal denaturation of the 10 amino acid long β hairpin protein. By completing a temperature dependent neutron scattering experiment, we will have access to structural details of the thermal denaturation of this model protein, including when the protein is fully folded, when the protein is at an intermediate unfolding state, and when the protein is completely unfolded. The results of these experiments will help in the understanding of the general mechanism of protein folding, particularly the formation of β sheets.