Near-Infrared spectra are strongly affected by hydrogen bonding. That means that a protein in its 'natural' state will have a distinctive spectrum in an aqueous solution. The secondary or tertiary structures of proteins, are determined by, in large part, hydrogen bonding. Disruption of this structure can lead to consequences from reduced food value to loss of activity in therapeutic materials such as insulin. As the structures are disrupted by temperature, salt concentration, or pH, the NIR spectra also change. Peaks can increase or decrease in intensity or shift to higher or lower frequencies with structural changes. These spectral changes may be measured and rates of reaction determined. The rates at which this denaturation occurs can allow suppliers and users to understand storage and/or use conditions.

Monitoring denaturation of soluble proteins by near infrared spectroscopy

244th National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.