FACILE TRANSITION BETWEEN 3(10)-HELIX AND ALPHA-HELIX - STRUCTURES OF8-RESIDUE, 9-RESIDUE, AND 10-RESIDUE PEPTIDES CONTAINING THE -(LEU-AIB-ALA)(2)-PHE-AIB- FRAGMENT
Il. Karle et al., FACILE TRANSITION BETWEEN 3(10)-HELIX AND ALPHA-HELIX - STRUCTURES OF8-RESIDUE, 9-RESIDUE, AND 10-RESIDUE PEPTIDES CONTAINING THE -(LEU-AIB-ALA)(2)-PHE-AIB- FRAGMENT, Protein science, 3(9), 1994, pp. 1547-1555
A structural transition from a 3(10)-helix to an alpha-helix has been
characterized at high resolution for an octapeptide segment located in
3 different sequences. Three synthetic peptides, decapeptide (A) Boc-
Aib-Trp-(Leu-Aib-Ala)(2)-Phe-Aib-OMe, nonapeptide (B) Boc-Trp-(Leu-Aib
-Ala)(2)-Phe-Aib-OMe, and octapeptide (C) Boc-(Leu-Aib-Ala)(2)-Phe-Aib
-OMe, are completely helical in their respective crystals. At 0.9 Angs
trom resolution, R factors for A, B, and C are 8.3%, 5.4%, and 7.3%, r
espectively. The octapeptide and nonapeptide form ideal 3(10)-helices
with average torsional angles Q(N-C-alpha) and psi(C-alpha-C') of -57
degrees, -26 degrees for C and -60 degrees, -27 degrees for B. The 10-
residue peptide (A) begins as a 3(10)-helix and abruptly changes to an
alpha-helix at carbonyl O(3), which is the acceptor for both a 4 -->
1 hydrogen bond with N(6)H and a 5 --> 1 hydrogen with N(7)H, even tho
ugh the last 8 residues have the same sequence in all 3 peptides. The
average phi,psi angles in the decapeptide are -58 degrees, -28 degrees
for residues 1-3 and -63 degrees, -41 degrees for residues 4-10. The
packing of helices in the crystals does not provide any obvious reason
for the transition in helix type. Fourier transform infrared studies
in the solid state also provide evidence for a 3(10)- to alpha-helix t
ransition with the amide I band appearing at 1,656-1,657 cm(-1) in the
9- and 10-residue peptides, whereas in shorter sequences the band is
observed at 1,667 cm(-1).