Wed, 20 Aug 2008 22:13:43 BST CiteULike: cjeans Elfstrom http://www.citeulike.org/user/cjeans/author/Elfstrom CiteULike.org en-gb Copyright © 2004-2008 citeulike.org http://www.citeulike.org/user/cjeans/article/2535240 <i>Proceedings of the National Academy of Sciences (13 March 2008), 0711732105.</i><br /><br />Understanding the molecular principles that govern allosteric communication is an important goal in protein science. One way allostery could be transmitted is via sparse energetic networks of residues, and one such evolutionary conserved network was identified in the PDZ domain family of proteins by multiple sequence alignment [Lockless SW, Ranganathan R (1999) Science 286:295299]. We have reassessed the energetic coupling of these residues by double mutant cycles together with ligand binding and stability experiments and found that coupling is not a special property of the coevolved network of residues in PDZ domains. The observed coupling for ligand binding is better explained by a distance relationship, where residues close in space are more likely to couple than distal residues. Our study demonstrates that statistical coupling from sequence analysis is not necessarily a reporter of energetic coupling and allostery. 10.1073/pnas.0711732105 Reassessing a sparse energetic network within a single protein domain Celestine Chi Lisa Elfstrom Yao Shi Tord Snall Ake Engstrom Per Jemth doi:10.1073/pnas.0711732105 Proceedings of the National Academy of Sciences (13 March 2008), 0711732105. 2008-03-15T01:25:34-00:00 2008 Proceedings of the National Academy of Sciences 0711732105 coevolution correlated-mutation domain sca