Table 4. Modified Gaussian Analysis of Orientations and Dynamics for Peptides of the GWALP23 Familya,b.
DLPC |
DOPC |
|||||||
---|---|---|---|---|---|---|---|---|
peptide | τ0 | ρ0 | σρ | RMSD (kHz) | τ0 | ρ0 | σρ | RMSD (kHz) |
W5 | 23 | 304 | 33 | 0.7 | 9 | 321 | 48 | 0.7 |
Y5 | 23 | 295 | 32 | 0.0 | 6 | 313 | 34 | 1.0 |
F5 | 17 | 314 | 21 | 1.7c | 9 | 329 | 40 | 0.6 |
Y4,5 | 14 | 259 | >90d | 1.7 | 6 | 344 | 72 | 0.9e |
F4,5 | 18 | 314 | 0f | 0.7 | 10 | 329 | 54 | 1.6 |
Y4 | 11 | 328 | 22 | 0.9 | 11 | 353 | 56 | 0.4 |
W5W18 | 18 | 35 | 8f | 1.4 | 17 | 264 | 50 | 1.2 |
The N-flanking aromatic residues are indicated by the abbreviation for each peptide. C-flanking W19 is also present in all samples except when the aromatic residues are W5 and W18.
Analysis followed Strandberg et al.,16 but στ was assigned a finite value instead of 0° (see Methods). Except as noted, στ was set to 15° in DLPC or 9° in DOPC.
The value of στ was 20° because no satisfactory solution was found when στ = 15°.
The value of σρ remains > 90° even if στ is set to 20°.
The value of στ was 13° because no satisfactory solution was found when στ = 9°.
The value of σρ is perhaps artificially low because of the choice of στ. Because of the limited data set, further solutions were not explored.