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Science 332 (6034): 1206-1209

Copyright © 2011 by the American Association for the Advancement of Science

Residue-Specific Vibrational Echoes Yield 3D Structures of a Transmembrane Helix Dimer

Amanda Remorino,1 Ivan V. Korendovych,2 Yibing Wu,2 William F. DeGrado,2 Robin M. Hochstrasser1,*

Abstract: Two-dimensional (2D) vibrational echo spectroscopy has previously been applied to structural determination of small peptides. Here we extend the technique to a more complex, biologically important system: the homodimeric transmembrane dimer from the α chain of the integrin αIIbβ3. We prepared micelle suspensions of the pair of 30-residue chains that span the membrane in the native structure, with varying levels of heavy (13C=18O) isotopes substituted in the backbone of the central 10th through 20th positions. The constraints derived from vibrational coupling of the precisely spaced heavy residues led to determination of an optimized structure from a range of model candidates: Glycine residues at the 12th, 15th, and 16th positions form a tertiary contact in parallel right-handed helix dimers with crossing angles of –58° ± 9° and interhelical distances of 7.7 ± 0.5 angstroms. The frequency correlation established the dynamical model used in the analysis, and it indicated the absence of mobile water associated with labeled residues. Delocalization of vibrational excitations between the helices was also quantitatively established.

1 Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104–6323, USA.
2 Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104–6059, USA.

* To whom correspondence should be addressed E-mail: hochstra{at}sas.upenn.edu


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Nonequilibrium dynamics of helix reorganization observed by transient 2D IR spectroscopy.
M. J. Tucker, M. Abdo, J. R. Courter, J. Chen, S. P. Brown, A. B. Smith III, and R. M. Hochstrasser (2013)
PNAS 110, 17314-17319
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