Evolutionarily conserved pathways of energetic connectivity in protein families

Steve W. Lockless, Rama Ranganathan

Research output: Contribution to journalArticlepeer-review

1043 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)295-299
Number of pages5
Issue number5438
StatePublished - Oct 8 1999

ASJC Scopus subject areas

  • General


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