Table 1 Summary of the helicity and morphologies.

The simulated and experimental helicity of pentapeptides examined in the present study and the morphologies of assemblies by these peptides according to simulations.

IDR1R2R4Computed
helicity
Computed
relative
helicity
Experiment
relative
helicity
SshapeSθ
1-MeAlaLeu0.71 ± 0.02*0.770.780.490.29
2-PhAlaLeu0.54 ± 0.090.590.590.390.35
3-MeLeuAla0.39 ± 0.080.42–†
4-PhLeuAla0.41 ± 0.090.450.480.39
5-MeAlaPhe0.27 ± 0.090.29
6-PhAlaPhe0.19 ± 0.050.210.270.380.38
7-MeAlaHpa0.68 ± 0.100.740.440.36
8-PhAlaHpa0.58 ± 0.080.630.650.530.32
9-MeAlaApp0.93 ± 0.031.010.620.35
10-PhAlaApp0.92 ± 0.061.001.000.970.06
11-MePheAla0.22 ± 0.070.24
12-PhPheAla0.26 ± 0.040.280.35
13-MeHpaAla0.34 ± 0.100.37
14-PhHpaAla0.30 ± 0.100.33
15-MeAppAla0.34 ± 0.090.370.590.39
16-PhAppAla0.42 ± 0.050.46
17-MeLeuLeu0.70 ± 0.060.760.370.32
18-PhLeuLeu0.66 ± 0.020.720.340.42
19-MeAppApp0.94 ± 0.081.020.250.36
20-PhAppApp0.82 ± 0.100.890.250.36
Derivatives of peptide 10
21Ala2Lys (A2K)0.86 ± 0.080.930.960.940.06
22Ala3Lys (A3K)0.95 ± 0.041.031.010.980.096
23Ala2Glu (A2E)0.94 ± 0.051.020.880.980.08
24Ala3Glu (A3E)0.95 ± 0.081.030.920.910.08

*Uncertainty was determined as absolute difference in predicted helicities between REMD runs starting with full helical and nonhelical structures.

†Not determined.

‡The results for peptides that can assemble into fiber segments are highlighted in boldface.