Report

Evolutionarily Conserved Pathways of Energetic Connectivity in Protein Families

See allHide authors and affiliations

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

You are currently viewing the abstract.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

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.

  • * To whom correspondence should be addressed. E-mail: rama{at}chop.swmed.edu

View Full Text