Competition between local conformational preferences and secondary structures in gas-phase model tripeptides as revealed by laser spectroscopy and theoretical chemistry

Chin, W.; Mons, Michel; Dognon, Jean-Pierre; Piuzzi, F.; Tardivel, B.; Dimicoli, I.

doi:10.1039/b315470j

Cited by 98 publications

(249 citation statements)

References 47 publications

Supporting

Mentioning

242

Contrasting

Order By: Relevance

“…Mons et al have also assigned the ''a phenyl orientation'' to the structure based on the Franck-Condon patterns in the REMPI spectrum. 29 For the spectrum shown in blue in Fig. 3, the assignment is not that straightforward.…”

Section: Conformational Assignmentmentioning

confidence: 99%

See 1 more Smart Citation

Can far-IR action spectroscopy combined with BOMD simulations be conformation selective?

Mahé

Jaeqx

Rijs

et al. 2015

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

show abstract

Section: Conformational Assignmentmentioning

confidence: 99%

“…3, the assignment is not that straightforward. This spectrum was previously assigned to a type VIa b-turn conformation with a cis conformation of the Phe-Pro peptide bond by Mons et al 29 The ''VIa'' is used to classify different types of b-turn conformations. This is also our conclusion from the present work.…”

Section: Conformational Assignmentmentioning

confidence: 99%

Can far-IR action spectroscopy combined with BOMD simulations be conformation selective?

Mahé

Jaeqx

Rijs

et al. 2015

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

show abstract

“…2,4,6,8,10,38 -40 In the case of the aromatic residues Trp and Phe, extended ␤-strandlike structures ͑referred to as ␤ L ) energetically compete with ␥-folds and are also observed experimentally. 31,32,35,36 Their stability results from the existence of a weak C 5 interaction between neighboring NH and CO moieties, resulting in an extended backbone, which also allows the formation of a stabilizing NH¯in-teraction between the aromatic ring and the trans NH of the C-terminal amide group. 35,41 Chart 1.…”

Section: Introductionmentioning

confidence: 99%

“…31,32,35,36 Their stability results from the existence of a weak C 5 interaction between neighboring NH and CO moieties, resulting in an extended backbone, which also allows the formation of a stabilizing NH¯in-teraction between the aromatic ring and the trans NH of the C-terminal amide group. 35,41 Chart 1. Possible intramolecular ͘NH¯OvC͗ interactions in the protected dipeptides studied.…”

Section: Introductionmentioning

confidence: 99%

“…After the pioneering work of Levy and co-workers on the amino acid tryptophan and its derivatives, 20 several experimental groups focused their efforts on other amino acids and peptides molecules, either having the N-and C-termini unmodified 24 -30 or chemically protected. [31][32][33][34][35][36] In particular, N-acetylated and C-amidated termini ͑chart 1͒ allow to study a͒ Author to whom correspondence should be addressed. Electronic mail: mmons@cea.fr the intrinsic folding properties of the peptide backbone as they introduce peptide bonds in the system.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Secondary structures of short peptide chains in the gas phase: Double resonance spectroscopy of protected dipeptides

Chin

Dognon

Canuel

et al. 2005

The Journal of Chemical Physics

Self Cite

162

View full text Add to dashboard Cite

The conformational structure of short peptide chains in the gas phase is studied by laser spectroscopy of a series of protected dipeptides, Ac-Xxx-Phe-NH 2 , XxxϭGly, Ala, and Val. The combination of laser desorption with supersonic expansion enables us to vaporize the peptide molecules and cool them internally; IR/UV double resonance spectroscopy in comparison to density functional theory calculations on Ac-Gly-Phe-NH 2 permits us to identify and characterize the conformers populated in the supersonic expansion. Two main conformations, corresponding to secondary structures of proteins, are found to compete in the present experiments. One is composed of a doubly ␥-fold corresponding to the 2 7 ribbon structure. Topologically, this motif is very close to a ␤-strand backbone conformation. The second conformation observed is the ␤-turn, responsible for the chain reversal in proteins. It is characterized by a relatively weak hydrogen bond linking remote NH and CO groups of the molecule and leading to a ten-membered ring. The present gas phase experiment illustrates the intrinsic folding properties of the peptide chain and the robustness of the ␤-turn structure, even in the absence of a solvent. The ␤-turn population is found to vary significantly with the residues within the sequence; the Ac-Val-Phe-NH 2 peptide, with its two bulky side chains, exhibits the largest ␤-turn population. This suggests that the intrinsic stabilities of the 2 7 ribbon and the ␤-turn are very similar and that weakly polar interactions occurring between side chains can be a decisive factor capable of controlling the secondary structure.

show abstract

Chirality‐Controlled Formation of β‐Turn Secondary Structures in Short Peptide Chains: Gas‐Phase Experiment versus Quantum Chemistry

Brenner¹,

Piuzzi²,

Dimicoli³

et al. 2007

Angewandte Chemie

Self Cite

View full text Add to dashboard Cite

Competition between local conformational preferences and secondary structures in gas-phase model tripeptides as revealed by laser spectroscopy and theoretical chemistry

Cited by 98 publications

References 47 publications

Can far-IR action spectroscopy combined with BOMD simulations be conformation selective?

Can far-IR action spectroscopy combined with BOMD simulations be conformation selective?

Secondary structures of short peptide chains in the gas phase: Double resonance spectroscopy of protected dipeptides

Chirality‐Controlled Formation of β‐Turn Secondary Structures in Short Peptide Chains: Gas‐Phase Experiment versus Quantum Chemistry

Contact Info

Product

Resources

About