Publications by Natalia Nagornova

Revealing the Structure of Tryptophan in Microhydrated Complexes by Cold Ion Spectroscopy

Natalia Nagornova, Andrei Zviagin, Ruslan Yamaletdinov, Manuel Dömer

The geometry of biomolecules isolated in the gas phaseusuallydiffers substantially from their native structures in aqueous solution,which are the only ones truly relevant to life science. To connectthe high resolution of cold ion spectroscopy that can be a ...

AMER CHEMICAL SOC2023

Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy

Vladimir Kopysov, Natalia Nagornova

The early stages of fibril formation are difficult to capture in solution. We use cold-ion spectroscopy to examine an 11-residue peptide derived from the protein transthyretin and clusters of this fibre-forming peptide containing up to five units in the ga ...

Wiley-Blackwell2018

A Decapeptide Hydrated by Two Waters: Conformers Determined by Theory and Validated by Cold Ion Spectroscopy

Natalia Nagornova, Robert Benny Gerber

The intrinsic structures of biomolecules in the gas phase may not reflect their native solution geometries. Microsolvation of the molecules bridges the two environments, enabling a tracking of molecular structural changes upon hydration at the atomistic le ...

American Chemical Society2017

The LOUVRE Laboratory: State-of-the-Art Ultrafast Ultraviolet Spectroscopies for Molecular and Materials Science

Majed Chergui, Natalia Nagornova, Frank van Mourik, Edoardo Baldini, Thomas Charles Henry Rossi, Malte Oppermann, Tania Palmieri, Lars-Hendrik Mewes, Benjamin Bauer, Aurelio Oriana

We describe the facilities for ultraviolet studies in the femtosecond to nanosecond time domain. These facilities consist of: i) a set-up for deep-ultraviolet spectroscopy in the 260-380 nm range in both pump and probe pulses for transient absorption/refle ...

Schweizerische Chemische Gesellschaft2017

The LOUVRE Laboratory: State-of-the-Art Ultrafast Ultraviolet Spectroscopies for Molecular and Materials Science

Majed Chergui, Natalia Nagornova, Frank van Mourik, Edoardo Baldini, Thomas Charles Henry Rossi, Malte Oppermann, Tania Palmieri, Lars-Hendrik Mewes, Benjamin Bauer, Aurelio Oriana

We describe the facilities for ultraviolet studies in the femtosecond to nanosecond time domain. These facilities consist of: i) a set-up for deep-ultraviolet spectroscopy in the 260–380 nm range in both pump and probe pulses for transient absorption/refle ...

2017

Vibrational Signatures of Conformer-Specific Intramolecular Interactions in Protonated Tryptophan

Natalia Nagornova, Aleksandr Pereverzev

Because of both experimental and computational challenges, protonated tryptophan has remained the last aromatic amino acid for which the intrinsic structures of low-energy conformers have not been unambiguously solved. The IR-IR UV hole-burning spectroscop ...

Amer Chemical Soc2016

Conformational Structures of a Decapeptide Validated by First Principles Calculations and Cold Ion Spectroscopy

Thomas Rizzo, Vladimir Kopysov, Natalia Nagornova, Robert Benny Gerber

Calculated structures of the two most stable conformers of a protonated decapeptide gramicidin S in the gas phase have been validated by comparing the vibrational spectra, calculat- ed from first- principles and measured in a wide spectral range using infr ...

Wiley-V C H Verlag Gmbh2015

Identification of Tyrosine-Phosphorylated Peptides Using Cold Ion Spectroscopy

Vladimir Kopysov, Natalia Nagornova

The accurate and unambiguous detection of post-translational modifications in proteins and peptides remains a challenging task. We report here the use of cold ion spectroscopy for the identification of phosphorylated tyrosine residues in peptides. This app ...

Amer Chemical Soc2014

Assessing the performance of computational methods for the prediction of the ground state structure of a cyclic decapeptide

Ursula Röthlisberger, Thomas Rizzo, Ivano Tavernelli, Natalia Nagornova, Matteo Guglielmi

We benchmark the performance of various computational approaches, ranging from the classical nonpolarizable force fields AMBER FF96 and FF99SB, the polarizable force fields AMBER FF02polEP and AMOEBAbio09 to the semiempirical DFT method SCC-DFTB. The test ...

Wiley-Blackwell2013

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Natalia Nagornova

Revealing the Structure of Tryptophan in Microhydrated Complexes by Cold Ion Spectroscopy

Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy

A Decapeptide Hydrated by Two Waters: Conformers Determined by Theory and Validated by Cold Ion Spectroscopy

The LOUVRE Laboratory: State-of-the-Art Ultrafast Ultraviolet Spectroscopies for Molecular and Materials Science

The LOUVRE Laboratory: State-of-the-Art Ultrafast Ultraviolet Spectroscopies for Molecular and Materials Science

Vibrational Signatures of Conformer-Specific Intramolecular Interactions in Protonated Tryptophan

Conformational Structures of a Decapeptide Validated by First Principles Calculations and Cold Ion Spectroscopy

Identification of Tyrosine-Phosphorylated Peptides Using Cold Ion Spectroscopy

Assessing the performance of computational methods for the prediction of the ground state structure of a cyclic decapeptide

Interplay of Intra- and Intermolecular H-Bonding in a Progressively Solvated Macrocyclic Peptide

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Vibrational Signatures of Conformer-Specific Intramolecular Interactions in Protonated Tryptophan

The LOUVRE Laboratory: State-of-the-Art Ultrafast Ultraviolet Spectroscopies for Molecular and Materials Science

The LOUVRE Laboratory: State-of-the-Art Ultrafast Ultraviolet Spectroscopies for Molecular and Materials Science

Identification of Tyrosine-Phosphorylated Peptides Using Cold Ion Spectroscopy

A Decapeptide Hydrated by Two Waters: Conformers Determined by Theory and Validated by Cold Ion Spectroscopy

Assessing the performance of computational methods for the prediction of the ground state structure of a cyclic decapeptide

Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy

Conformational Structures of a Decapeptide Validated by First Principles Calculations and Cold Ion Spectroscopy

Interplay of Intra- and Intermolecular H-Bonding in a Progressively Solvated Macrocyclic Peptide

Revealing the Structure of Tryptophan in Microhydrated Complexes by Cold Ion Spectroscopy