ArticleJournal of the American Chemical Society2006
Transfer of structural elements from compact to extended states in unsolvated ubiquitin.
Article in Journal of the American Chemical Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Accessing Different Protein Conformer Ensembles with Tunable Capillary Vibrating Sharp-Edge Spray Ionization.The journal of physical chemistry. B · 2025Article
- Structure and Stabilities of Solution and Gas Phase Protein Complexes.Journal of the American Society for Mass Spectrometry · 2024Article
- Metastability of Protein Solution Structures in the Absence of a Solvent: Rugged Energy Landscape and Glass-like Behavior.Journal of the American Chemical Society · 2024Article
- Elucidating Structures of Protein Complexes by Collision-Induced Dissociation at Elevated Gas Pressures.Journal of the American Society for Mass Spectrometry · 2023Article
- Perspective on the potential of tandem-ion mobility /mass spectrometry methods for structural proteomics applications.Frontiers in analytical science · 2023Article
- Protein Unfolding in Freeze Frames: Intermediate States are Revealed by Variable-Temperature Ion Mobility-Mass Spectrometry.Analytical chemistry · 2022Article
- Influence of N Terminus Amino Acid on Peptide Cleavage in Solution through Diketopiperazine Formation.Journal of the American Society for Mass Spectrometry · 2022Article
- Tandem-trapped ion mobility spectrometry/mass spectrometry (The Analyst · 2022Review
- Diketopiperazine Formation from FPGThe journal of physical chemistry. B · 2021Article
- Influence of Solvents upon Diketopiperazine Formation of FPGThe journal of physical chemistry. B · 2021Article
- Comment on Effective Temperature and Structural Rearrangement in Trapped Ion Mobility Spectrometry.Analytical chemistry · 2020Article
- On the Preservation of Non-covalent Peptide Assemblies in a Tandem-Trapped Ion Mobility Spectrometer-Mass Spectrometer (TIMS-TIMS-MS).Journal of the American Society for Mass Spectrometry · 2019Article
- Optimizing Native Ion Mobility Q-TOF in Helium and Nitrogen for Very Fragile Noncovalent Structures.Journal of the American Society for Mass Spectrometry · 2018Article
- Melting proteins confined in nanodroplets with 10.6 μm light provides clues about early steps of denaturation.Chemical communications (Cambridge, England) · 2018Article
- The Solution Assembly of Biological Molecules Using Ion Mobility Methods: From Amino Acids to Amyloid β-Protein.Annual review of analytical chemistry (Palo Alto, Calif.) · 2017Review
- From Compact to String-The Role of Secondary and Tertiary Structure in Charge-Induced Unzipping of Gas-Phase Proteins.Journal of the American Society for Mass Spectrometry · 2017Article
- Molecular Structures and Momentum Transfer Cross Sections: The Influence of the Analyte Charge Distribution.Journal of the American Society for Mass Spectrometry · 2017Article
- Action-FRET of a Gaseous Protein.Journal of the American Society for Mass Spectrometry · 2017Article
- Charge-Induced Unzipping of Isolated Proteins to a Defined Secondary Structure.Angewandte Chemie (International ed. in English) · 2016Article
- Infrared Spectroscopy of Mobility-Selected H+-Gly-Pro-Gly-Gly (GPGG).Journal of the American Society for Mass Spectrometry · 2015Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Multidimensional ion mobility spectrometry techniques (IMS-IMS and IMS-IMS-IMS) combined with mass spectrometry are used to study structural transitions of ubiquitin ions in the gas phase. It is possible to select and activate narrow distributions of compact and partially folded conformation types and examine new distributions of structures that are formed. Different compact conformations unfold, producing a range of new partially folded states and three resolvable peaks associated with elongated conformers. Under gentle activation conditions, the final populations of the three elongated forms depend on the initial structures of the selected ions. This requires that some memory of the compact state (most likely secondary structure) is preserved along the unfolding pathway. Activation of selected, partially folded intermediates (formed from specific compact states) leads to elongated state populations that are consistent with the initial selected compact form-evidence that intermediates not only retain elements of initial structure but also are capable of transmitting structure to final states.
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