Tuesday, September 13, 2011

HSP60: How Do Our Proteins Fold?

Dr. Arthur Horwich, A medical geneticist here at Yale University just won an award for his work on and discovery of HSP60, a protein that acts as a "changing room" of sorts for other proteins. Newly formed proteins enter the HSP60 where they can fold themselves into their final functional shape.

As we know, proteins start out as a polypeptide. According to an experiment by the biochemist Christian Anfinsen in the 1950s, the amino acids' own attractions and repulsions were the sole force creating the protein's final shape. Contrarily, Dr. Horwich found that proteins could not always fold themselves correctly on their own. He discovered that though HSP60 does not "grab a protein and fold it like an origami master . . . it gives the protein the isolation it needs to fold itself" correctly.

This discovery could lead to cures for multiple diseases. One such illness, Alzheimer's, in which people "develop clumps of tangled proteins in their brains," has been projected by a group from Johns Hopkins University to affect one out of every eighty-five individuals worldwide by the year 2050.

Read more about Dr. Horwich and his work in the New York Times article "Horwich Wins Lasker Award . . ."

Learn more about the protein itself at PhosphoSitePlus.

View the Johns Hopkins study here.

View information and renderings of proteins at Protein Data Bank Japan.

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