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Native ion mobility-mass spectrometry and related methods in structural biology.

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TLDR
This overview article will describe these methods and highlight some recent applications for proteins and protein complexes, with particular emphasis on native MS analysis.
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The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics

TL;DR: Ion mobility-mass spectrometry can be used to gain insights into the conformational dynamics of a system, offering a unique means of characterizing flexibility and folding mechanisms.
Journal ArticleDOI

Oligosaccharide analysis by mass spectrometry: A review of recent developments

TL;DR: This review covers developments in the application of mass spectrometry to the analysis of carbohydrates, with an emphasis on work that has occurred from January 2011 through October 2013.
Journal ArticleDOI

Recommendations for reporting ion mobility Mass Spectrometry measurements

TL;DR: A guide to ion mobility mass spectrometry experiments, which covers both linear and nonlinear methods: what is measured, how the measurements are done, and how to report the results, including the uncertainties of mobility and collision cross section values.
Journal ArticleDOI

Cross-Linking Mass Spectrometry: An Emerging Technology for Interactomics and Structural Biology.

TL;DR: Strategies to Overcome Inherent Challenges in XLMS Studies and their Applications.
Journal ArticleDOI

Collision cross sections for structural proteomics.

TL;DR: IMACT (Ion Mobility Projection Approximation Calculation Tool), which overcomes the lack of speed at which structures and models can be related to experimental data and demonstrates that the CCS is a highly informative parameter and that IM-MS is of considerable practical value to structural biologists.
References
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Journal ArticleDOI

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide.

TL;DR: Findings in other neurodegenerative diseases indicate that a broadly similar process of neuronal dysfunction is induced by diffusible oligomers of misfolded proteins.
Journal ArticleDOI

Analytical properties of the nanoelectrospray ion source.

TL;DR: Improved desolvation in nanoES led to instrument-limited resolution of the signals of a glycoprotein and the ability to signal average extensively allowed the C-terminal sequencing of a 40 kDa protein.
Journal ArticleDOI

Electrospray ionization–principles and practice

TL;DR: Electrospray (E S ) ionization has recently shown itself capable of producing intact ions, with multiple charges, from remarkably large, complex, and fragile parent species as mentioned in this paper, which is the state-of-the-art in mass spectrometric analysis.
Journal ArticleDOI

Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation

TL;DR: Results of this investigation indicate that the combination of protein fragmentation and HPLC‐FABMS is relatively free of constraints associated with other analytical methods used for this purpose and may be a general method for determining hydrogen exchange rates in specific segments of proteins.
Journal ArticleDOI

Ion mobility-mass spectrometry analysis of large protein complexes.

TL;DR: Within this protocol, general approaches to data interpretation, methods of predicting whether specific model structures for a given protein assembly can be separated by ion mobility, and generalized strategies for data normalization and modeling are covered.
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