A Yale researcher has discovered that it is not necessary for proteins to have a greasy core in order for the critical process known as protein folding to occur.

This discovery represents a whole new way of looking at these critical molecules.

"Protein folding is now a major subject in biochemistry and biophysics that has many ramifications for normal cells and for disease," says Donald Engelman, the Eugene Higgins Professor of Molecular Biophysics and Biochemistry, whose study is published in the Jan. 27 issue of Nature magazine. "In some diseases it appears proteins that don't fold correctly are involved."

In fact, scientists believe that alternatively folded proteins may be a factor in adult-onset diabetes and Alzheimer's disease, he notes.

Until now, it was thought that proteins organized themselves in one way: The proteins first formed a long stringy polypeptide, then collapsed to a compact shape by separating their oily parts from water, and then organized themselves to make detailed functional structures.

What is new here is the concept that a protein can organize itself differently, without the use of this hydrophobic, collapsed mechanism.

Engelman's collaborator was Shohei Koide of the University of Rochester Medical Center.

The investigators studied and modified the structure of a protein that has a region that does not seem to have what was believed to be the essential hydrophobic core.

"So, there is at least one alternative way of folding a protein without this feature that everyone thought was the key," Engelman says. "This is a paradigm shift."

-- BY JACQUELINE WEAVER

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