Structural insights into charge pair interactions in triple helical collagen-like proteins.

ABSTRACT: 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 and solution state. Structures from x-ray crystallography may have similarities to the densely packed triple helices of collagen fibers whereas solution NMR structures reveal the simpler interactions of isolated triple helices. In soluti

SUBMITTER: Fallas JA 

PROVIDER: S-EPMC3318716 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature