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Solution NMR Evidence for Symmetry in Functionally or Crys-tallographically Asymmetric Homodimers

Published

Author(s)

David Travis Gallagher, Raquel Godoy-Ruiz, Anna Krejcirikova, Vitali Tugarinov

Abstract

A recurrent theme of many structural studies of homo-oligomeric protein systems is concerned with verification that the conformation observed in a crystal repre¬sents the functionally relevant structure. An asymmetric con-formation adopted by two chemically identical subunits in homo-oligomers can represent an intrinsic property of a protein or be an artifact induced by crystal packing forces. Solution NMR studies can distinguish between these two possibilities. Using methyl-based NMR spectroscopy we provide evidence for symmetry in the absence of ligands in several homodimeric proteins that are either asymmetric functionally and/or adopt different conformations of the two subunits in available x-ray structures.
Citation
Journal of the American Chemical Society
Volume
133
Issue
49

Keywords

NMR, CRP, Symmetry, Crystallography

Citation

Gallagher, D. , Godoy-Ruiz, R. , Krejcirikova, A. and Tugarinov, V. (2011), Solution NMR Evidence for Symmetry in Functionally or Crys-tallographically Asymmetric Homodimers, Journal of the American Chemical Society, [online], https://doi.org/10.1021/ja206967d (Accessed March 4, 2024)
Created October 18, 2011, Updated March 14, 2023