Continuous flow reduced‐pressure infrared laser desorption/ionization mass spectrometry

Iguchi, Yasunari; Hazama, Hisanao; Awazu, Kunio

doi:10.1002/rcm.7970

Cited by 1 publication

(1 citation statement)

References 28 publications

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“…In particular since last year, the scientific community is becoming aware of the LILBID technique [ 11 – 14 ] and some groups already implementing ion sources which are based on LILBID or quite close to it [ 15 – 17 ].…”

Section: Introductionmentioning

confidence: 99%

LILBID and nESI: Different Native Mass Spectrometry Techniques as Tools in Structural Biology

Peetz

Hellwig

Henrich

et al. 2018

J. Am. Soc. Mass Spectrom.

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Native mass spectrometry is applied for the investigation of proteins and protein complexes worldwide. The challenge in native mass spectrometry is maintaining the features of the proteins of interest, such as oligomeric state, bound ligands, or the conformation of the protein complex, during transfer from solution to gas phase. This is an essential prerequisite to allow conclusions about the solution state protein complex, based on the gas phase measurements. Therefore, soft ionization techniques are required. Widely used for the analysis of protein complexes are nanoelectro spray ionization (nESI) mass spectrometers. A newer ionization method is laser induced liquid bead ion desorption (LILBID), which is based on the release of protein complexes from solution phase via infrared (IR) laser desorption. We use both methods in our lab, depending on the requirements of the biological system we are interested in. Here we benchmark the performance of our LILBID mass spectrometer in comparison to a nESI instrument, regarding sample conditions, buffer and additive tolerances, dissociation mechanism and applicability towards soluble and membrane protein complexes. Graphical Abstract ᅟ.

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Section: Introductionmentioning

confidence: 99%