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New paper #59: Ribosome gate

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We have another paper (paper #59 at http://folding.stanford.edu/English/Papers)


by Paula M. Petrone, Christopher D. Snow, Del Lucent, and Vijay S. Pande.  Proceedings of the National Academy of Sciences, USA


which recently was published, representing a major step for FAH. 


This one deals with the ribosome. The ribosome is a fascinating molecular machine, responsible for the synthesis of proteins. For this reason it is of fundamental importance to protein folding (as the last step in the central dogma of biology) as well as to human health (since the ribosome is the target of a very large fraction of antibiotics). One of the questions revolving around ribosome function is why is there a large tunnel inside the ribosome, through which proteins exit after being synthesized. In this paper, we used "bigWU" classic clients (clients which allow larger systems to run) since the ribosome is so huge that it would not run on regular classic clients.


 The primary goal of this paper was to analyze the surface of the ribosome tunnel. Understanding the nature of this surface would be useful for both understanding the fundamental nature of protein synthesis as well as how key antibiotics interact with the ribosome. An interesting related discovery was the identification of a potential "ribosome gate" which can open and close selectively, based on what is interacting with the gate. This suggests novel hypotheses for several aspects of ribosome function as well as interesting new directions for work on studying the ribosome and for new routes for antibiotics.




Voir l'article complet

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