Observation of water molecules bound to a protein using cold-spray ionization mass spectrometry

Anal Sci. 2005 Apr;21(4):449-51. doi: 10.2116/analsci.21.449.

Abstract

The characterization of water molecules bound to ribonuclease T1 (RNase T1) was carried out using cold-spray ionization mass spectrometry (CSI-MS). CSI-MS is a variant of electrospray ionization mass spectrometry (ESI-MS) operating at low temperature, and is particularly suitable for investigating the weaker molecular associations, since the temperature at the spray interface is much lower than that in the conventional ESI-MS. In this approach, ion peaks due to the addition of nine water molecules were identified at a spray temperature of 48 degrees C. This result showed good agreement with that inferred by the combinational analysis of NMR and X-ray crystallography, indicating that CSI-MS is capable of rapidly providing reliable information to characterize the number of water molecules bound to a macromolecule.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Escherichia coli / enzymology
  • Protein Binding
  • Ribonuclease T1 / chemistry*
  • Spectrometry, Mass, Electrospray Ionization
  • Water / chemistry*

Substances

  • Water
  • Ribonuclease T1