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Biotechnology Techniques

, Volume 8, Issue 3, pp 199–202 | Cite as

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

  • Timothy J. Hancock
  • James T. Hsu
Article

Abstract

The melting point of several poly(ethylene glycols) (PEGs) was used to calibrate the temperature above ambient with the separation of the hydroxyl and methylene peaks of ethylene glycol (EG) on a 500 MHz nuclear magnetic resonance (NMR) 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, useful for protein stability studies.

Keywords

Methylene Hydroxyl Nuclear Magnetic Resonance Ethylene Glycol Melting Point 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Science & Technology Letters 1994

Authors and Affiliations

  • Timothy J. Hancock
    • 1
  • James T. Hsu
    • 1
  1. 1.Department of Chemical EngineeringLehigh University, Iacocca HallBethlehemUSA

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