IM-MS for Supramolecular Systems: Structures and Dynamics of Noncovalent Complexes From Solution to Gas Phase

Tae Su Choi; Jongcheol Seo; Hugh I. Kim

doi:10.1016/bs.coac.2018.09.002

IM-MS for Supramolecular Systems: Structures and Dynamics of Noncovalent Complexes From Solution to Gas Phase

Tae Su Choi, Jongcheol Seo, Hugh I. Kim

Research output: Chapter in Book/Report/Conference proceeding › Chapter

1 Citation (Scopus)

Abstract

Ion mobility mass spectrometry (IM-MS) has been broadly utilized in the structural characterization of noncovalent, supramolecular complexes. In this chapter, we discuss three types of supramolecular complexes, and their structural dynamics observed in IM-MS studies. Firstly, host–guest chemistry of cucurbituril, crown ether, and cyclodextrin is discussed. Secondly, self-assembly mechanisms of amino acids and peptides are introduced. Finally, structural studies of protein–protein complexes are presented. We mainly focus on insights into the physicochemical properties of supramolecular complexes (e.g. molecular interactions, role of water molecules in complexation and structural features).

Original language	English
Title of host publication	Comprehensive Analytical Chemistry
Publisher	Elsevier B.V.
Pages	197-236
Number of pages	40
DOIs	https://doi.org/10.1016/bs.coac.2018.09.002
Publication status	Published - 2019 Jan 1

Publication series

Name	Comprehensive Analytical Chemistry
Volume	83
ISSN (Print)	0166-526X

Keywords

Host–guest chemistry
Ion mobility mass spectrometry
Protein–protein complex
Self-assembly

ASJC Scopus subject areas

Analytical Chemistry
Spectroscopy

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title = "IM-MS for Supramolecular Systems: Structures and Dynamics of Noncovalent Complexes From Solution to Gas Phase",

abstract = "Ion mobility mass spectrometry (IM-MS) has been broadly utilized in the structural characterization of noncovalent, supramolecular complexes. In this chapter, we discuss three types of supramolecular complexes, and their structural dynamics observed in IM-MS studies. Firstly, host–guest chemistry of cucurbituril, crown ether, and cyclodextrin is discussed. Secondly, self-assembly mechanisms of amino acids and peptides are introduced. Finally, structural studies of protein–protein complexes are presented. We mainly focus on insights into the physicochemical properties of supramolecular complexes (e.g. molecular interactions, role of water molecules in complexation and structural features).",

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T2 - Structures and Dynamics of Noncovalent Complexes From Solution to Gas Phase

AU - Choi, Tae Su

AU - Seo, Jongcheol

AU - Kim, Hugh I.

PY - 2019/1/1

Y1 - 2019/1/1

N2 - Ion mobility mass spectrometry (IM-MS) has been broadly utilized in the structural characterization of noncovalent, supramolecular complexes. In this chapter, we discuss three types of supramolecular complexes, and their structural dynamics observed in IM-MS studies. Firstly, host–guest chemistry of cucurbituril, crown ether, and cyclodextrin is discussed. Secondly, self-assembly mechanisms of amino acids and peptides are introduced. Finally, structural studies of protein–protein complexes are presented. We mainly focus on insights into the physicochemical properties of supramolecular complexes (e.g. molecular interactions, role of water molecules in complexation and structural features).

AB - Ion mobility mass spectrometry (IM-MS) has been broadly utilized in the structural characterization of noncovalent, supramolecular complexes. In this chapter, we discuss three types of supramolecular complexes, and their structural dynamics observed in IM-MS studies. Firstly, host–guest chemistry of cucurbituril, crown ether, and cyclodextrin is discussed. Secondly, self-assembly mechanisms of amino acids and peptides are introduced. Finally, structural studies of protein–protein complexes are presented. We mainly focus on insights into the physicochemical properties of supramolecular complexes (e.g. molecular interactions, role of water molecules in complexation and structural features).

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KW - Ion mobility mass spectrometry

KW - Protein–protein complex

KW - Self-assembly

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