Mechanisms of UV Photodissociation of Small Protonated Peptides

Pérot, Marie; Lucas, Bruno; Barat, M.; Fayeton, J. A.; Jouvet, Christophe

doi:10.1021/jp908937s

Cited by 33 publications

(68 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Studies of the 263 nm UVPD behavior of protonated Trp and Trp-containing dipeptides suggest that fragments arise from cleavage of ions in excited electronic states following hydrogen transfer and by internal conversion and subsequent dissociation via CID-like pathways. 50,51 One possibility for the unusual behavior observed here is that internal conversion and vibrational energy re-distribution following 193 nm photoabsorption is particularly prevalent at Trp residues, resulting in unusually abundant b and a ions from more conventional CID-type pathways. It is noteworthy that several of the experimental α a values for melittin, such as those for Lys7, Val8, Leu9, and Leu13, were found to be much lower than the HB means associated with UV photoactivated cleavages at those residues.…”

Section: Resultsmentioning

confidence: 98%

Characterization of hydrogen bonding motifs in proteins: hydrogen elimination monitoring by ultraviolet photodissociation mass spectrometry

Morrison

Chai

Rosenberg

et al. 2017

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

Determination of structure and folding of certain classes of proteins remains intractable by conventional structural characterization strategies and has spurred the development of alternative methodologies. Mass spectrometry-based approaches have a unique capacity to differentiate protein heterogeneity due to the ability to discriminate populations, whether minor or major, featuring modifications or complexation with non-covalent ligands on the basis of m/z. Cleavage of the peptide backbone can be further utilized to obtain residue-specific structural information. Here, hydrogen elimination monitoring (HEM) upon ultraviolet photodissociation (UVPD) of proteins transferred to the gas phase via nativespray ionization is introduced as an innovative approach to deduce backbone hydrogen bonding patterns. Using well-characterized peptides and a series of proteins, prediction of the engagement of the amide carbonyl oxygen of the protein backbone in hydrogen bonding using UVPD-HEM is demonstrated to show significant agreement with the hydrogen-bonding motifs derived from molecular dynamics simulations and X-ray crystal structures.

show abstract

Section: Resultsmentioning

confidence: 98%

Characterization of hydrogen bonding motifs in proteins: hydrogen elimination monitoring by ultraviolet photodissociation mass spectrometry

Morrison

Chai

Rosenberg

et al. 2017

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

show abstract

“…For gramicidin S this problem was overcome by detecting specific fragments arising from prompt dissociation on an electronically excited surface subsequent to UV excitation. While this seems to occur when using aromatic amino acids as chromophores [86,99,129,150,181,182], it may not be general for all biomolecules.…”

Section: +mentioning

confidence: 99%

Cryogenic Methods for the Spectroscopy of Large, Biomolecular Ions

Rizzo

Boyarkin

2014

Topics in Current Chemistry

View full text Add to dashboard Cite

Determining the conformation of biological molecules is key for understanding their function. The recent combination of mass spectrometry, cryogenic ion traps, and laser spectroscopy is providing new methods to interrogate individual conformations of peptides and proteins that have advantages over classical techniques of structure determination. This chapter provides an overview of these new state-of-the-art methods and illustrates several specific applications. After reviewing the fundamentals of ion production, trapping, cooling, and spectroscopic detection, we review how different combinations of these techniques have been implemented in various laboratories around the world. We then focus on applications of cryogenic ion spectroscopy from two specific laboratories to illustrate the potential of this general approach. Finally, we outline ways in which these powerful new techniques could be further improved.

show abstract

“…During this process, the retinal chromophore of the opsin protein absorbs a photon and subsequently undergoes ultrafast IC facilitated by conical intersections, leading to photoisomerization [6,7] which changes the conformation of the protein and induces a neural signal. Ultrafast IC is also responsible for avoiding harmful photochemical reactions of DNA [8,9] and proteins, [10][11][12][13] protecting organisms from UV radiation. IC is also present in the photochemistry of small molecules, for example O 2 and O 3 , [14] SO 2 , [15] NO 2 , [16] and other nitrogen oxides.…”

Section: Introductionmentioning

confidence: 99%

A general method to describe intersystem crossing dynamics in trajectory surface hopping

Mai

Marquetand

González

2015

Int J of Quantum Chemistry

271

406

View full text Add to dashboard Cite

Intersystem crossing is a radiationless process that can take place in a molecule irradiated by UV‐Vis light, thereby playing an important role in many environmental, biological and technological processes. This paper reviews different methods to describe intersystem crossing dynamics, paying attention to semiclassical trajectory theories, which are especially interesting because they can be applied to large systems with many degrees of freedom. In particular, a general trajectory surface hopping methodology recently developed by the authors, which is able to include nonadiabatic and spin‐orbit couplings in excited‐state dynamics simulations, is explained in detail. This method, termed SHARC, can in principle include any arbitrary coupling, what makes it generally applicable to photophysical and photochemical problems, also those including explicit laser fields. A step‐by‐step derivation of the main equations of motion employed in surface hopping based on the fewest‐switches method of Tully, adapted for the inclusion of spin‐orbit interactions, is provided. Special emphasis is put on describing the different possible choices of the electronic bases in which spin‐orbit can be included in surface hopping, highlighting the advantages and inconsistencies of the different approaches. © 2015 Wiley Periodicals, Inc.

show abstract

Mechanisms of UV Photodissociation of Small Protonated Peptides

Cited by 33 publications

References 30 publications

Characterization of hydrogen bonding motifs in proteins: hydrogen elimination monitoring by ultraviolet photodissociation mass spectrometry

Characterization of hydrogen bonding motifs in proteins: hydrogen elimination monitoring by ultraviolet photodissociation mass spectrometry

Cryogenic Methods for the Spectroscopy of Large, Biomolecular Ions

A general method to describe intersystem crossing dynamics in trajectory surface hopping

Contact Info

Product

Resources

About