SIMPLE METHOD FOR SAMPLE TEMPERATURE CALIBRATION IN A 500 MHZ NMR SPECTROMETER USEFUL FOR PROTEIN STUDIES

Authors
Citation
Tj. Hancock et Jt. Hsu, SIMPLE METHOD FOR SAMPLE TEMPERATURE CALIBRATION IN A 500 MHZ NMR SPECTROMETER USEFUL FOR PROTEIN STUDIES, Biotechnology techniques, 8(3), 1994, pp. 199-202
Citations number
13
Categorie Soggetti
Biothechnology & Applied Migrobiology
Journal title
ISSN journal
0951208X
Volume
8
Issue
3
Year of publication
1994
Pages
199 - 202
Database
ISI
SICI code
0951-208X(1994)8:3<199:SMFSTC>2.0.ZU;2-S
Abstract
The melting point of several poly (ethylene glycols) (PEGs) was used t o calibrate the temperature above ambient with the separation of the h ydroxyl and methylene peaks of ethylene glycol (EG) on a 500 MHz nucle ar magnetic resonance (NMR) spectrometer. The calibration is almost id entical to a calibration of the EG sample on a 90 MHz NMR spectrometer using a thermocouple. The equation accurately predicts the thermal de naturation midpoint of the protein, hen egg white lysozyme. It is conc luded that in the absence of a small magnet, the calibration of an EG sample using the melting points of PEGs provides a sample temperature calibration, for larger superconducting magnets, useful for protein st ability studies.