Isolated Neutral Peptides

Gloaguen, Éric; Mons, Michel

doi:10.1007/128_2014_580

Cited by 42 publications

(95 citation statements)

References 224 publications

(488 reference statements)

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“…17 Studying peptide aggregation under neutral conditions might provide more insights into non-charge driven aggregation interactions, such as dispersion interactions, NH-p and p-p stacking, and intra-and intermolecular hydrogen bond interactions. [23][24][25][26] For example, the p-p interactions are expected to play a directing role by stabilizing the hydrophobic domains crucial for the development of amyloid structures. 24,[27][28][29][30][31] Although cluster formation between (bio)molecules and solvent molecules, such as water or methanol, is rather straightforward by co-expanding the solvent molecules with the seed gas, [32][33][34][35] the formation of aggregates of neutral peptides is not.…”

Section: Introductionmentioning

confidence: 99%

Interactions of aggregating peptides probed by IR-UV action spectroscopy

et al. 2019

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Section: Introductionmentioning

confidence: 99%

Interactions of aggregating peptides probed by IR-UV action spectroscopy

et al. 2019

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“…At T~450 K, the relative electronic energies for the most populous structures fall into the interval of 2 to 3 kcal/mol. Notice that T~450 K is often expected for the relevant experimental conditions such as laser heating 23 , 24 . Therefore, conformers within a sufficiently large energy range of the global minimum should be thoroughly searched in order to reliably determine the most important conformers under the experimental condition.…”

Section: Resultsmentioning

confidence: 99%

“…The single-point energy calculations were carried out using the functional DSD-PBEP86-D3BJ with the basis set of aug-cc-pVTZ. The functional M062X is used here as it is capable of describing H-bonds well at a reasonable calculation cost 20 , 24 , 33 . The functional DSD-PBEP86-D3BJ is known to describe H-bond systems with accuracy close to that of CCSD(T) and is used here to provide high quality conformational energies 34 , 35 .…”

Section: Discussionmentioning

confidence: 99%

Computational study on single molecular spectroscopy of tyrosin-glycine, tryptophane-glycine and glycine-tryptophane

Yang

Liu

Lin

2017

Sci Rep

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Quantum chemistry calculations play a fundamental role in revealing the molecular structures observed in gas-phase spectroscopic measurements. The supersonic jet cooling widely used in single molecular spectroscopy experiment is a non-equilibrium process and often causes confusion on the theoretical and experimental comparison. A computational approach is proposed here to account for the effect of the non-equilibrium cooling on the experimental spectra and applied to the cases of tyrosin-glycine (YG), tryptophane-glycine (WG) and glycine-tryptophane (GW). The low energy conformers of YG, WG and GW are obtained through thorough conformational searches. The structural features and equilibrium distributions of conformations and the energy barriers for conformer conversions are then determined. Three classes of transition energy barriers, high, medium and low, are found for the conversions among conformers with distinctly different, similar and the same structural types, respectively. The final conformation populations are determined by assuming an initial temperature of about 450 K and allowing for only the conformation conversion with a low energy barrier to occur during the rapid cooling process. The results provide a natural explanation for the numbers of YG, WG and GW conformations observed experimentally. The theoretical conformation assignments are also in good agreement with the experimental IR data.

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“…Conformer-specific measurements are essential to unequivocally connect the photophysical behavior of a peptide and its structure. For an overview of experimental achievements, the reader is advised to consult some of excellent experimental reviews [ 20 , 21 , 22 , 23 ]. The description of the experimental setups and relevant measurements performed on the systems under investigation can be found in [ 17 , 24 , 25 ].…”

Section: General Aspectsmentioning

confidence: 99%

Nonradiative Relaxation Mechanisms of UV Excited Phenylalanine Residues: A Comparative Computational Study

Mališ

Došlić

2017

Molecules

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The present work is directed toward understanding the mechanisms of excited state deactivation in three neutral model peptides containing the phenylalanine residue. The excited state dynamics of the γL(g+) folded form of N-acetylphenylalaninylamide (NAPA B) and its amide-N-methylated derivative (NAPMA B) is reviewed and compared to the dynamics of the monohydrated structure of NAPA (NAPAH). The goal is to unravel how the environment, and in particular solvation, impacts the photodynamics of peptides. The systems are investigated using reaction path calculations and surface hopping nonadiabatic dynamics based on the coupled cluster doubles (CC2) method and time-dependent density functional theory. The work emphasizes the role that excitation transfer from the phenyl ππ* to amide nπ* state plays in the deactivation of the three systems and shows how the ease of out-of-plane distortions of the amide group determines the rate of population transfer between the two electronic states. The subsequent dynamics on the nπ* state is barrierless along several pathways and leads to fast deactivation to the ground electronic state.

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Isolated Neutral Peptides

Cited by 42 publications

References 224 publications

Interactions of aggregating peptides probed by IR-UV action spectroscopy

Interactions of aggregating peptides probed by IR-UV action spectroscopy

Computational study on single molecular spectroscopy of tyrosin-glycine, tryptophane-glycine and glycine-tryptophane

Nonradiative Relaxation Mechanisms of UV Excited Phenylalanine Residues: A Comparative Computational Study

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