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Biophysics: A curious puzzle about protein folding …

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From the Weizmann Institute of Science, via Science Blogs (November 14, 2011): A protein could take one of several paths through its folding landscape:

The team identified six different intermediate configurations for the protein they studied. Sometimes the strands went through all of them; other times, they took an easier, shorter route to their final form.

Why would a molecule go through extra contortions to get to the same state? The findings contain a clue: The process became longer and more tortuous in the presence of some external factors such as heat or higher concentrations of certain chemicals in the protein’s environment.

Like much good research, this study raises more questions than it answers: Is this a general rule that holds for different types of proteins? What advantages do the different routes to protein structure confer? How this might tie into such disorders as Alzheimer’s disease, in which badly-folded proteins form plaques in brain tissue?

2 Replies to “Biophysics: A curious puzzle about protein folding …

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    Protein folding is a huge area of important research. I think many people have the impression that proteins fold automatically, based on nothing more than the attractions between the amino acids. More and more, scientists are discovering that the folding process is coordinated, orchestrated. Among other implications, this means that the cell has to contain, not just the specified sequence in its DNA for a particular protein, but algorithms for how the resulting chain of amino acids is to be folded (and machinery to do so). Yet another level of carefully orchestrated functional complexity.

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