The collagen triple helix is the most abundant protein fold in humans. Despite its deceptively
simple structure, very little is understood about its folding and fibrillization energy landscape.
In this work, using a combination of x-ray crystallography and nuclear magnetic resonance
spectroscopy, we carry out a detailed study of stabilizing pair-wise interactions between the
positively charged lysine and the negatively charged amino acids aspartate and glutamate.
We find important differences in the side chain conformation of amino acids in the crystalline …