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Biophys. J. BioFAST: First Published January 14, 2005. doi:10.1529/biophysj.104.047639
© 2005 by the Biophysical Society.

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PROTEINS

A Vibrational Spectral Maker for Probing the Hydrogen Bonding Status of Protonated Asp and Glu Residues

Beining Nie 1, Jerrod Stutzman 1 and Aihua Xie 1*

1 Oklahoma State University

* To whom correspondence should be addressed. E-mail: xaihua{at}okstate.edu.

Submitted on June 28, 2004
Revised on August 10, 2004
Accepted on 20 December 2004


  Abstract
Hydrogen bonding is a fundamental element in protein structure and function. Breaking a single hydrogen bond may impair the stability of a protein. We report an infrared vibrational spectral marker for probing the hydrogen-bond number for buried, protonated Asp or Glu residues in proteins. Ab initio computational studies were performed on hydrogen bonding interactions of a COOH group with a variety of side chain model compounds of polar and charged amino acids in vacuum using density function theory. For hydrogen bonding interactions with polar side chain groups, our results show a strong correlation between the C=O stretching frequency and the hydrogen bond number of a COOH group: ~1759 to1776 cm-1 for zero, ~1733 to 1749 cm-1 for one, and 1703 to 1710 cm-1 for two hydrogen bonds. Experimental evidence for this correlation will be discussed. In addition, we show an approximate linear correlation between the C=O stretching frequency and the hydrogen-bond strength. We propose that a two-dimensional infrared spectroscopy, C=O stretching vs. O-H stretching, may be employed to identify the specific type of hydrogen bonding interaction. This vibrational spectral marker for hydrogen bonding interaction is expected to enhance the power of time-resolved Fourier transform infrared spectroscopy for structural characterization of functionally important intermediates of proteins.

Key Words: 2D infrared spectroscopy, Fourier transform infrared spectroscopy, butyric acid, density functional theory, hydrogen bond, proton transfer




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Copyright © 2005 by the Biophysical Society.