Nonnative interactions regulate folding and switching of myristoylated protein.

Abstract

We present an integrated experimental and computational study of the molecular mechanisms by which myristoylation affects protein folding and function, which has been little characterized to date. Myristoylation, the covalent linkage of a hydrophobic C14 fatty acyl chain to the N-terminal glycine in a protein, is a common modification that plays a critical… (More)
DOI: 10.1073/pnas.1201803109

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