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Evolutionarily Conserved Pathways of Energetic Connectivity in Protein Families

Science  08 Oct 1999:
Vol. 286, Issue 5438, pp. 295-299
DOI: 10.1126/science.286.5438.295

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Abstract

For mapping energetic interactions in proteins, a technique was developed that uses evolutionary data for a protein family to measure statistical interactions between amino acid positions. For the PDZ domain family, this analysis predicted a set of energetically coupled positions for a binding site residue that includes unexpected long-range interactions. Mutational studies confirm these predictions, demonstrating that the statistical energy function is a good indicator of thermodynamic coupling in proteins. Sets of interacting residues form connected pathways through the protein fold that may be the basis for efficient energy conduction within proteins.

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