Evolutionarily Conserved Pathways of Energetic Connectivity in Protein Families
- 8 October 1999
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 286 (5438), 295-299
- https://doi.org/10.1126/science.286.5438.295
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.Keywords
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