Protein Folding and Misfolding
The content you've requested is available without charge only to active Sigma Xi members and affiliates.
If you are an active member, affiliate or individual subscriber, please log in now in order to access this article. Be sure you've entered your member or subscriber number on your profile page.
If you are not a member, affiliate or individual subscriber, you can:
Abstract:
Protein chains can fold into an enormous range of structures, but a few basic localized folds, or secondary structures, are widespread. The most common of these are alpha helices and beta sheets. The sequence of amino acids in a protein generally determines its three-dimensional shape, but researchers are still struggling to decipher the underlying grammar that links sequence to structure. Even understanding the formation of a basic beta-sheet structure has been difficult. Amino acids that make up a structure are often far apart in sequence, and understanding their long-range chemical interactions is an intricate problem. Recent experiments with one protein—the tailspike protein of a virus that infects Salmonella—have contributed a great deal to the understanding of how a specific kind of beta-sheet structure, the beta coil, forms. This is a step toward solving the protein-folding problem—or how sequence determines fold. This remains an important problem to solve since the precise folding of a cell’s thousands of proteins is crucial to their function and a cell’s life.