Publication: 2D-IR spectroscopy of the sulfhydryl band of cysteines in the hydrophobic core of proteins
2D-IR spectroscopy of the sulfhydryl band of cysteines in the hydrophobic core of proteins
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Kozinski, M., Garrett-Roe, S., & Hamm, P. (2008). 2D-IR spectroscopy of the sulfhydryl band of cysteines in the hydrophobic core of proteins. Journal of Physical Chemistry. B, 112(25), 7645–7650. https://doi.org/10.1021/jp8005734
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We investigate the sulfhydryl band of cysteines as a new chromophore for two-dimensional IR (2D-IR) studies of the structure and dynamics of proteins. Cysteines can be put at almost any position in a protein by standard methods of site-directed mutagenesis and, hence, have the potential to be an extremely versatile local probe. Although being a very weak absorber in aqueous environment, the sulfhydryl group gets strongly polarized when situated in an alpha-helix inside the hydrophobic core of a protein because of a strong hydrogen bon
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- Kozinski, M
- Garrett-Roe, S
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Kozinski, M., Garrett-Roe, S., & Hamm, P. (2008). 2D-IR spectroscopy of the sulfhydryl band of cysteines in the hydrophobic core of proteins. Journal of Physical Chemistry. B, 112(25), 7645–7650. https://doi.org/10.1021/jp8005734
