Date:1/11/2013

t forward by Janin and Sternberg, Dunker and Uversky conclude that the major difference between ordinary proteins and IDPs is that the former fold first and then bind to their partners while that latter remain disordered until they bind their partners. Furthermore, some IDPs can be much more dynamic than just "waiting for a partner", with the ability to switch from one partner to another and change structures while changing the partner.

Commenting on the two articles, Richard Henderson, MRC Laboratory of Molecular Biology, Cambridge said: "Both articles are by leaders who have given a great deal of thought to the function of proteins that appear to be intrinsically unfolded. Their different emphases will no doubt stimulate experiments as well as debate in the Structural Biology community. Time will tell us whether one or both models reflect how nature uses these structures."

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Contact: Eleanor Howell press@f1000.com 44-020-763-19129 Faculty of 1000: Biology and Medicine Source:Eurekalert

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