Structure and Conformation of Protonated d -(+)-Biotin in the Unsolvated State
| Autor: | Laura Guarcini, Antonello Filippi, Maurizio Speranza, Caterina Fraschetti, Vincent Steinmetz |
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| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular Spectrometry Mass Electrospray Ionization Quantitative Biology::Biomolecules Proton Chemistry Folded structure Molecular Conformation Biotin Hydrogen Bonding Protonation State (functional analysis) biotin IRMPD gas-phase molecular conformation Surfaces Coatings and Films Gas phase Crystallography chemistry.chemical_compound Materials Chemistry Gases Infrared multiphoton dissociation Protons Physical and Theoretical Chemistry Conformational isomerism |
| Zdroj: | The Journal of Physical Chemistry B. 119:6198-6203 |
| ISSN: | 1520-5207 1520-6106 |
| DOI: | 10.1021/acs.jpcb.5b02660 |
| Popis: | A combined computational and infrared multiphoton dissociation (IRMPD) spectroscopic investigation shows that protonated d-(+)-biotin, formed in the gas phase by ESI-MS, acquires a folded structure with proton bonding between the ureido and valeryl carbonyls, and that only a single conformer of such a structure predominates. A uniform frequency vs distance correlation function is proposed for the O(+)-H···O and N-H···O bonds involved in the folded conformers of O2'-protonated d-(+)-biotin in the gas phase which, therefore, depends exclusively on the corresponding geometric parameters. |
| Databáze: | OpenAIRE |
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