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. 2014 May 14;53(22):3637–3645. doi: 10.1021/bi500439x

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
a

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.

b

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.

c

The value of στ was 20° because no satisfactory solution was found when στ = 15°.

d

The value of σρ remains > 90° even if στ is set to 20°.

e

The value of στ was 13° because no satisfactory solution was found when στ = 9°.

f

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.