Tandem-trapped ion mobility spectrometry/mass spectrometry (<i>t</i>TIMS/MS): a promising analytical method for investigating heterogenous samples-Reference-Cited by-同舟云学术

Tandem-trapped ion mobility spectrometry/mass spectrometry (tTIMS/MS): a promising analytical method for investigating heterogenous samples

Published:2022 Issue:11 Volume:147 Page:2317-2337
ISSN:0003-2654
Container-title:The Analyst
language:en
Short-container-title:Analyst

Author:

Liu Fanny C.¹^ORCID,Ridgeway Mark E.²,Park Melvin A.²,Bleiholder Christian¹³

Affiliation:

1. Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32306-4390, USA

2. Bruker Daltonics Inc., Billerica, MA 01821, USA

3. Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306-4390, USA

Abstract

This review focuses on the instrumental development and potential applications of Tandem-Trapped Ion Mobility Spectrometry/Mass Spectrometry (tTIMS/MS) for protein structure elucidation.

Funder

National Institute of General Medical Sciences

National Science Foundation

Publisher

Royal Society of Chemistry (RSC)

Subject

Electrochemistry,Spectroscopy,Environmental Chemistry,Biochemistry,Analytical Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2022/AN/D2AN00335J

Reference152 articles.

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3. Structural Analysis of the Glycoprotein Complex Avidin by Tandem-Trapped Ion Mobility Spectrometry–Mass Spectrometry (Tandem-TIMS/MS)

4. Structure Relaxation Approximation (SRA) for Elucidation of Protein Structures from Ion Mobility Measurements

5. Comment on Effective Temperature and Structural Rearrangement in Trapped Ion Mobility Spectrometry

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