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Exact(5)

The peptides showed a more helical structure as the concentration of membrane-mimetic solution increased.

Novel concepts are introduced to suggest an internal ventricular patch can be used as an intercavitary curtain, through covering nonscarred septa1 muscle (ie, normal but distended) to amplify left ventricular function through producing a more helical structure.

From a grand total of 5 μs of implicit solvent replica-exchange molecular dynamics, we conclude that under folding conditions segments 1 and 4 form more helical structure and orient correctly relative to the native structure more often than do segments 2 and 3. Helices 1 and 2 retain the most residual structure and orientation at high temperatures.

One-dimensional and two-dimensional proton NMR and electron microscopy studies performed on the peptide in DMSO/H2O solution with different ratios indicate that the peptide monomer tends to adopt a more helical structure during the hydrogelation as the DMSO/H2O ratio is reduced.

However comparisons of the CD spectra of the protein in high salt ([8] and unpublished results) suggest that the protein may have an even slightly more helical structure under those conditions, in line with studies on other ion channels that have shown that the presence of permeating or blocking ions may act to order and stabilise channels [42 44].

Similar(55)

These NMR data indicate formation of a stable α-helix in the C-terminal part of the F1 loop and a more transient helical structure in the N-terminal region, correlating well with the higher helical propensity in the C-terminal region in the absence of TFE.

Helical structure-forming propensity further influenced this window of selective antifungal activity, with more stable helical structures eliciting specificity for C. albicans over a broader range of hydrophobicity.

From Table 2, it is clear to see that N-terminal amino acids in the peptide P sequence may be more important to stabilize the helical structure since the relative helicity values of peptide K7D/K14D (71.7%) and L6D/L12D (73.1%) were lower than those of the peptide K14D/K22D (81%) and L12D/L20D (75.7%) respectively.

When the pH was increased from pH10.6 to pH12 (Fig. 7B), the lysines on d-EAK16 became de-protonated and the structure became more helical.

Molecular dynamics simulation studies confirm that P11-6 peptide maintains relatively stable helical structure and exerts more perturbation action on the order of acyl tail of lipid bilayer.

It is interesting to see that, single L-lysine on the polar face had more important role to sustain the helical structure than L-leucine on the non-polar face due to the relative helicity values of single D-amino acid substituted peptides K7D (77.8%), K14D (88.7%) and K22D (85.5%) were less than those of L6D (99.6%), L12D (95.1%) and L20D (92.9%), respectively.

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