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Water Penetration into Protein Secondary Structure Revealed by Hydrogen−Deuterium Exchange Two-Dimensional Infrared Spectroscopy

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Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139
Cite this: J. Am. Chem. Soc. 2006, 128, 51, 16520–16521
Publication Date (Web):December 7, 2006
https://doi.org/10.1021/ja067723o
Copyright © 2006 American Chemical Society
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    Abstract

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    Two-dimensional infrared spectroscopy in conjunction with hydrogen−deuterium exchange experiments provides detailed information about solvent penetration into protein structure. Correlating the secondary-structure sensitivity of the amide I vibration and the solvent-exposure sensitivity of amide II provides a direct probe of solvent-inaccessible residues of proteins embedded in the hydrophobic core or those involved in strong hydrogen bonds in secondary structures. Distinct spectral signatures of the cross-peak region arising from the coupling of the amide I and II modes imply a significant degree of structural stability of hydrogen-bonded contacts in α-helices and β-sheets in a series of proteins. Ubiquitin, an α/β-protein, exhibits strong α-helical signatures and lacks those of the β-sheet in the cross-peak region, demonstrating that ubiquitin's β-sheet exchanges protons with the surrounding solvent and is conformationally unstable.

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    Sample preparation; data analysis; and additional 2D spectra of lysozyme, serum albumin, β-lactoglobulin, and partially and fully exchanged ubiquitin. This material is available free of charge via the Internet at http:// pubs.acs.org.

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