Protein Conformational Stability Probed by Fourier Transform Ion Cyclotron Resonance Mass Spectrometry
β Scribed by Eyles, Stephen J.; Speir, J. Paul; Kruppa, Gary H.; Gierasch, Lila M.; Kaltashov, Igor A.
- Book ID
- 121409974
- Publisher
- American Chemical Society
- Year
- 2000
- Tongue
- English
- Weight
- 140 KB
- Volume
- 122
- Category
- Article
- ISSN
- 0002-7863
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The experimental Fourier transform ion cyclotron resonance (FT/ICR) frequency range has been extended to 107 MHz. We report the observation of FT/ICR signals from electron-ionized species of mass-to-charge ratio 8, 7, 6, 5, 4, 3, 2, and 1 ΞΌ per elementary charge. We show that moderately high charge
Two-dimensional Fourier transform (2D FT) spectroscopy is applied to ion cyclotron resonance (ICR) to obtain direct evidence for mass transfer due to ion-molecule collisions. The 2D FI ICR experiment, which is closely analogous to 2D exchange NMR spectroscopy (NOESY), yields similar information to t