Untangling The Protein Folding Problem

Accounts Of Chemical Research Special Report

Scientists are gaining ground in their effort to solve the long-standing "protein folding problem" -- deciphering the elusive chemical code that determines the three-dimensional structure of proteins. The ability to predict the final folded form of a protein will advance efforts to design new drugs and decode genetic information obtained from the Human Genome Project, among other things.

The latest efforts toward unraveling the mysteries of protein folding are reported in a special edition of Accounts of Chemical Research, a monthly peer- reviewed journal published by the American Chemical Society, the world's largest scientific society. The special report, due out in print on Nov. 18, includes results of research done at laboratories in England, Sweden and the U.S.

Protein folding research is "undergoing explosive growth," according to an editorial by Jay Winkler, Ph.D., and Harry Gray, Ph.D., both chemists at the California Institute of Technology and guest editors for the special issue. "Protein folding was once considered an almost intractable problem," write Winkler and Gray, but new efforts "are beginning to reveal the secrets of this prototypal spontaneous self-assembly process."

The special journal issue focuses on the chemical kinetics of the folding phenomenon -- the rate of change as the protein assumes its three-dimensional structure -- and includes a study on recent efforts to make "real time" observations. Folding happens very quickly, which makes it difficult to observe.

For some proteins, the change occurs in milliseconds (thousandths of a second); for others, it can be even faster. Despite recent progress toward understanding the mechanisms of protein folding, scientists still don't agree on exactly how it happens, as evidenced in the journal by the differing conclusions of several articles about the same protein.

"That each of these has a different interpr

Contact: Marvin Coyner
American Chemical Society

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