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- Thomas Wyttenbach
- Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106;
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- Nicholas A. Pierson
- Department of Chemistry, Indiana University, Bloomington, Indiana 47405;
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- David E. Clemmer
- Department of Chemistry, Indiana University, Bloomington, Indiana 47405;
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- Michael T. Bowers
- Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106;
説明
<jats:p> The combination of mass spectrometry and ion mobility spectrometry (IMS) employing a temperature-variable drift cell or a drift tube divided into sections to make IMS-IMS experiments possible allows information to be obtained about the molecular dynamics of polyatomic ions in the absence of a solvent. The experiments allow the investigation of structural changes of both activated and native ion populations on a timescale of 1–100 ms. Five different systems representing small and large, polar and nonpolar molecules, as well as noncovalent assemblies, are discussed in detail: a dinucleotide, a sodiated polyethylene glycol chain, the peptide bradykinin, the protein ubiquitin, and two types of peptide oligomers. Barriers to conformational interconversion can be obtained in favorable cases. In other cases, solution-like native structures can be observed, but care must be taken in the experimental protocols. The power of theoretical modeling is demonstrated. </jats:p>
収録刊行物
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- Annual Review of Physical Chemistry
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Annual Review of Physical Chemistry 65 (1), 175-196, 2014-04-01
Annual Reviews