Nonlinear optical properties of flavylium salts: a quantum chemical study.

Ab initio calculations have been carried out to unravel the relationships between the structure and the first hyperpolarizability in flavylium derivatives, with the aim to design efficient second-order nonlinear optical (NLO) switching compounds. Large contrasts of the first hyperpolarizability have been obtained along the pH-controlled and photoinduced transformations for specific combinations of chemical substituents in the 4'- and 7-positions, which demonstrates that these multistate systems should behave as highly efficient molecular NLO switches.

Modelling the influence of hydrogen bond network on chemical shielding tensors description. GIAO-DFT study of WALP23 transmembrane alpha-helix as a test case.

Density Functional Theory (B3LYP/6-31G(d,p)) calculations of (15)N amide and (13)C carbonyl NMR chemical shielding tensors have been performed on WALP23trans-membrane alpha-helix peptide and compared to solid state NMR experiment performed on [(13)C(1)-Ala(13), (15)N-Leu(14)] specifically labelled peptide powder sample. Using either theoretical results obtained on the whole peptide or experimental data as reference, several simplest chemical models have been explored in order to reduce the computational cost while maintaining good theoretical accuracy. From this study, it appears that the hydrogen bond (N-H...O=C) network that exists in the alpha-helix has a major influence on the chemical shielding tensor and more specifically on the carbonyl (13)C sigma(22) eigenvalue. We show that a small truncated WALP_7 model is not adequate for (13)C(1) NMR description. The application of an external electric field in order to model the hydrogen bond network allows calculating chemical shielding tensors with accurate eigenvalues while the associated eigenvectors are largely modified. Finally, a 23 residues polyglycine peptide that includes the Alanine and Leucine residues for which NMR parameters must be calculated is proposed as the chemical model. This model is sufficient to mostly reproduce the calculation performed on WALP23 with major gain in computational time. Moreover, the application of a low intensity external electric field allows reaching the experimental accuracy for the determination of the eigenvalues.

Order parameters of a transmembrane helix in a fluid bilayer: case study of a WALP peptide.

A new solid-state NMR-based strategy is established for the precise and efficient analysis of orientation and dynamics of transmembrane peptides in fluid bilayers. For this purpose, several dynamically averaged anisotropic constraints, including (13)C and (15)N chemical shift anisotropies and (13)C-(15)N dipolar couplings, were determined from two different triple-isotope-labeled WALP23 peptides ((2)H, (13)C, and (15)N) and combined with previously published quadrupolar splittings of the same peptide. Chemical shift anisotropy tensor orientations were determined with quantum chemistry. The complete set of experimental constraints was analyzed using a generalized, four-parameter dynamic model of the peptide motion, including tilt and rotation angle and two associated order parameters. A tilt angle of 21 degrees was determined for WALP23 in dimyristoylphosphatidylcholine, which is much larger than the tilt angle of 5.5 degrees previously determined from (2)H NMR experiments. This approach provided a realistic value for the tilt angle of WALP23 peptide in the presence of hydrophobic mismatch, and can be applied to any transmembrane helical peptide. The influence of the experimental data set on the solution space is discussed, as are potential sources of error.