Simple method for sample temperature calibration in a 500 MHz NMR spectrometer useful for protein studies

✍ Scribed by Timothy J. Hancock; James T. Hsu

• Book ID: 104649616
• Publisher: Springer-Verlag
• Year: 1994
• Tongue: English
• Weight: 329 KB
• Volume: 8
• Category: Article
• ISSN: 0951-208X
• DOI: 10.1007/bf00161590

✦ Synopsis

The melring point of several poly(ethylene glycols) (PEGS) was used to calibrate rhe temperature above ambient with the separation of the hydroxyl and methylene peaks of ethylene glycol (EG) on a 500 MHz nuclear magnetic resonance (Nh4R) spectrometer. The calibration is almost identical to a calibration of the EG sample on a 90 MHz NMR spectrometer using a thermocouple. The equation accurately predicts the thermal denaturation midpoint of the protein, hen egg white lysozyme. It is concluded that in the absence of a small magnet, the calibration of an EG sample using the melting points of PEGS provides a simple temperature calibration, for larger superconducting magnets, usefilforprotein stability studies.