title: Ion mobility analysis of molecular dynamics.
abstract: 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.
authors: Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106; email: bowers@chem.ucsb.edu.
authors: Thomas
authors: T
authors: Wyttenbach
authors: Nicholas A
authors: NA
authors: Pierson
authors: David E
authors: DE
authors: Clemmer
authors: Michael T
authors: MT
authors: Bowers
mesh_terms: D000818:Animals; D006801:Humans; D007477:Ions / Q000737:chemistry; D013058:Mass Spectrometry / Q000379:methods*; D056004:Molecular Dynamics Simulation; D010455:Peptides / Q000737:chemistry; D011108:Polymers / Q000737:chemistry; D011506:Proteins / Q000737:chemistry
chemical_list: D007477:Ions; D010455:Peptides; D011108:Polymers; D011506:Proteins