Measuring The Effects of Sugar on Hydrogen Bonding in Water through Infrared Spectroscopy
Presentation Type
Poster
Faculty Advisor
Johannes Schelvis
Access Type
Event
Start Date
26-4-2024 11:15 AM
End Date
26-4-2024 12:15 PM
Description
At temperatures exceeding 70 ℃, thermophiles demonstrate remarkable hyperthermostability, enabling their proteins to maintain structural integrity even under extreme temperatures. Co-solvents, small alcohols in sugars, have been identified as crucial players in enhancing protein stability among thermophiles, effectively preserving isolated proteins in their presence. By measuring their effects on the water vibrational spectrum, these co-solvents can help us understand their effects on water and hydrogen bonding. The use of infrared spectroscopy reveals that ��-glycerophosphate modifies hydrogen bonding in water the most, whereas sucrose has a smaller effect and trehalose has a negligible effect.
Measuring The Effects of Sugar on Hydrogen Bonding in Water through Infrared Spectroscopy
At temperatures exceeding 70 ℃, thermophiles demonstrate remarkable hyperthermostability, enabling their proteins to maintain structural integrity even under extreme temperatures. Co-solvents, small alcohols in sugars, have been identified as crucial players in enhancing protein stability among thermophiles, effectively preserving isolated proteins in their presence. By measuring their effects on the water vibrational spectrum, these co-solvents can help us understand their effects on water and hydrogen bonding. The use of infrared spectroscopy reveals that ��-glycerophosphate modifies hydrogen bonding in water the most, whereas sucrose has a smaller effect and trehalose has a negligible effect.