scholarly journals Concentration‐dependent coulombic effects in travelling wave ion mobility spectrometry collision cross section calibration

2020 ◽  
Author(s):  
Charles Eldrid ◽  
Eloise O'Connor ◽  
Konstantinos Thalassinos
Keyword(s):  
Cross Section ◽  
Ion Mobility Spectrometry ◽  
Ion Mobility ◽  
Collision Cross Section ◽  
Travelling Wave

Characterisation of Calmodulin Structural Transitions by Ion Mobility Mass Spectrometry

2012 ◽  
Vol 65 (5) ◽  
pp. 504 ◽  
Author(s):  
Antonio N. Calabrese ◽  
Lauren A. Speechley ◽  
Tara L. Pukala
Keyword(s):  
Mass Spectrometry ◽  
Cross Section ◽  
Cross Sections ◽  
Ion Mobility ◽  
Collision Cross Section ◽  
Travelling Wave ◽  
Ion Mobility Mass Spectrometry ◽  
Structural Transitions ◽  
Calmodulin Binding ◽  
Negative Mode

This study demonstrates the ability of travelling wave ion mobility-mass spectrometry to measure collision cross-sections of ions in the negative mode, using a calibration based approach. Here, negative mode ion mobility-mass spectrometry was utilised to understand structural transitions of calmodulin upon Ca2+ binding and complexation with model peptides melittin and the plasma membrane Ca2+ pump C20W peptide. Coexisting calmodulin conformers were distinguished on the basis of their mass and cross-section, and identified as relatively folded and unfolded populations, with good agreement in collision cross-section to known calmodulin geometries. Titration of calcium tartrate to physiologically relevant Ca2+ levels provided evidence for intermediately metalated species during the transition from apo- to holo-calmodulin, with collision cross-section measurements indicating that higher Ca2+ occupancy is correlated with more compact structures. The binding of two representative peptides which exemplify canonical compact (melittin) and extended (C20W) peptide-calmodulin binding models has also been interrogated by ion mobility mass spectrometry. Peptide binding to calmodulin involves intermediates with metalation states from 1–4 Ca2+, which demonstrate relatively collapsed structures, suggesting neither the existence of holo-calmodulin or a pre-folded calmodulin conformation is a prerequisite for binding target peptides or proteins. The biological importance of the different metal unsaturated calmodulin complexes, if any, is yet to be understood.

Collision cross section prediction of deprotonated phenolics in a travelling-wave ion mobility spectrometer using molecular descriptors and chemometrics

2016 ◽  
Vol 924 ◽  
pp. 68-76 ◽  
Author(s):  
Gerard Bryan Gonzales ◽  
Guy Smagghe ◽  
Sofie Coelus ◽  
Dieter Adriaenssens ◽  
Karel De Winter ◽  
...  
Keyword(s):  
Cross Section ◽  
Ion Mobility ◽  
Molecular Descriptors ◽  
Collision Cross Section ◽  
Travelling Wave ◽  
Ion Mobility Spectrometer

scholarly journals Travelling Wave Ion Mobility-Derived Collision Cross Section for Mycotoxins: Investigating Interlaboratory and Interplatform Reproducibility

2020 ◽  
Vol 68 (39) ◽  
pp. 10937-10943
Author(s):  
Laura Righetti ◽  
Nicola Dreolin ◽  
Alberto Celma ◽  
Mike McCullagh ◽  
Gitte Barknowitz ◽  
...  
Keyword(s):  
Cross Section ◽  
Ion Mobility ◽  
Collision Cross Section ◽  
Travelling Wave

scholarly journals Modular calibrant sets for the structural analysis of nucleic acids by ion mobility spectrometry mass spectrometry

The Analyst ◽  
2016 ◽  
Vol 141 (13) ◽  
pp. 4084-4099 ◽  
Author(s):  
Jennifer L. Lippens ◽  
Srivathsan V. Ranganathan ◽  
Rebecca J. D'Esposito ◽  
Daniele Fabris
Keyword(s):  
Mass Spectrometry ◽  
Nucleic Acid ◽  
Structural Analysis ◽  
Nucleic Acids ◽  
Cross Section ◽  
Ion Mobility Spectrometry ◽  
Ion Mobility ◽  
Collision Cross Section ◽  
Calibration Curves

This study explored the use of modular nucleic acid (NA) standards to generate calibration curves capable of translating primary ion mobility readouts into corresponding collision cross section (CCS) data.

scholarly journals Sequence-specific model for predicting peptide collision cross-section values in proteomic ion mobility spectrometry

2020 ◽  
Author(s):  
Chih-Hsiang Chang ◽  
Darien Yeung ◽  
Victor Spicer ◽  
Oleg Krokhin ◽  
Yasushi Ishihama
Keyword(s):  
Cross Section ◽  
Ion Mobility Spectrometry ◽  
Ion Mobility ◽  
Collision Cross Section ◽  
Specific Model ◽  
Peptide Sequence ◽  
Preferential Formation ◽  
Charge Solvation ◽  
Peptide Helicity ◽  
Peptide Charge

ABSTRACTThe contribution of peptide amino-acid sequence to collision cross-section values (CCS) has been investigated using a dataset of ∼134,000 peptides of four different charge states (1+ to 4+). The migration data was acquired using a two-dimensional LC/trapped ion mobility spectrometry/quadrupole/time-of-flight MS analysis of HeLa cell digests created using 7 different proteases and was converted to CCS values. Following the previously reported modeling approaches using intrinsic size parameters (ISP), we extended this methodology to encode the position of individual residues within a peptide sequence. A generalized prediction model was built by dividing the dataset into 8 groups (four charges for both tryptic/non-tryptic peptides). Position dependent ISPs were independently optimized for the eight subsets of peptides, resulting in prediction accuracy of ∼0.981 for the entire population of peptides. We find that ion mobility is strongly affected by the peptide’s ability to solvate the positively charged sites. Internal positioning of polar residues and proline leads to decreased CCS values as they improve charge solvation; conversely, this ability decreases with increasing peptide charge due to electrostatic repulsion. Furthermore, higher helical propensity and peptide hydrophobicity result in preferential formation of extended structures with higher than predicted CCS values. Finally, acidic/basic residues exhibit position dependent ISP behaviour consistent with electrostatic interaction with the peptide macro-dipole, which affects the peptide helicity.

Interlaboratory and Interplatform Study of Steroids Collision Cross Section by Traveling Wave Ion Mobility Spectrometry

2020 ◽  
Vol 92 (7) ◽  
pp. 5013-5022 ◽  
Author(s):  
Maykel Hernández-Mesa ◽  
Valentina D’Atri ◽  
Gitte Barknowitz ◽  
Mathieu Fanuel ◽  
Julian Pezzatti ◽  
...  
Keyword(s):  
Cross Section ◽  
Ion Mobility Spectrometry ◽  
Ion Mobility ◽  
Traveling Wave ◽  
Collision Cross Section ◽  
Traveling Wave Ion Mobility
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