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. 2007 Jan 23;4(15):587–606. doi: 10.1098/rsif.2006.0203

Table 1.

Torsion angle parameters observed in crystallographically determined turn structures involving ω-amino acid residues. βVal, β valine; βPhe, β phenylalanine; Aib, α-aminoisobutyric acid; ACPC, trans-2-aminocyclopentanecarboxylic acid; β-Gly, β glycine; Dec, (2S,4S,6S)-2-amino-6-hydroxy-4-methyl-8-odxe-ocanoic acid; MHA, (4S, 2E)-4-methylhex-2-enoic acid; DPDA, (2S)-N,N-dimethylpropane-l,2-diamine; Me Pro, Methyl proline; HyLeu, hydroxyleucine; DAP, diamino pimelic acid; β-Res1, 8-aminocyclooct-4-enecarboxylic acid; Gpn, Gabapentin, (1-(aminomethyl) cyclohexaneacetic acid); γAbu, γ-aminoisobutyric acid; γ-Res Z, 2, 2 di-fluoro,3-oxo,4-methyl γ-aminoisobutyric acid; γ-ResX, 3-methoxy, 4-methyl γ-aminoisobutyric acid; γ-ResY, 4-methyl, 2–3 eneyl γ-aminoisobutyric acid; β-Res A, 2-benzyl, 3-(thio phenyl)methyl β-glycine; β-Res B, 3-ethyl,2-methyl β-glycine; Nip, nipecotic acid; δAva, δ aminovaleric acid; γ-Res A, 2-benzyl, 4-methyl γ-aminoisobutyric acid; γ-Res B, 4-isopropyl, 2-methyl γ-aminoisobutyric acid; γ- Res C, 2-, 3-, 4-trimethyl, γ-aminoisobutyric acid and γ-Res D, 2-isopropyl, 3-,4- dimethyl γ-aminoisobutyric acid.

peptide/reference turn type residue torsion angles (deg.) analogous α-turn
ϕ θ1 θ2 θ3 ψ
αβ-turns (C11)
Boc-Val-Alu-Phe-Aib-βVal-βPhe-Aib-Val-Alu-Phe-Aib-OMe/Roy et al. (2004) βα β-Phe 6 −88 80 — — −118 type III
Aib 7 −55 — — — −49
Boc-(Aib-trans ACPC)4-OBz/Schmitt et al. (2005) βαa trans ACPC −95.8 94.5 — — −89.9 type III
Aib −53.5 — — −39.9
Boc-β-Gly-Aib-Leu-Aib-OMe/Banerjee et al. (2003) βα βGly1 −103.8 83.7 — — − 84.7 type III
Aib 2 −56.1 — −44.6
Boc-(trans ACPC-trans ACPC-Phe)2OMe/Schmitt et al. (2006) βα trans ACPC 2 −67.5 105.8 — — −129.8 type III
Phe 3 −69.9 — — — −23.1
Boc-(trans ACPC-Aib-Aib)2-OMe/Schmitt et al. (2006) βαb trans ACPC −89.2 89.2 — — −94.3 type III
Aib −54.6 — — −32.3
Boc-(trans ACPC- transACPC-Phe)2OMe/Schmitt et al. (2006) αβ Phe 3 −69.9 — — — −23.1 type III
trans ACPC 4 −112.5 74.9 — — 163.0
Boc-Aib-Aib-βGly-NHMe/Pavone et al. (1992) αβc Aib 2 −64.8 — — — −13.52 type III
βGly 3 −88.8 70.9 — — −101.3
Boc-(Aib-trans ACPC)4-OBz/Schmitt et al. (2005) αβa Aib −53.9 — — — −41.2 type III
trans ACPC −95.8 94.5 — — −89.9
MHA-MePro-Dec-HyLeu-Leu-Leu-Aib-Aib-βGly-DPDA, Cerrini et al. (1989) αβ Aib 8 −66.8 — — — −49.2 type III
βGly 9 −103.3 79.7 — — −78.5
Boc-(trans ACPC-Aib-Aib)2-OMe/Schmitt, et al. (2006) αβ Aib3 −52.0 — — — −40.0 type III
trans ACPC 4 −95.0 95.8 — — −85.1
Boc-Aib-βRes1-Aib-OMe/Tanaka et al. (2001) αβ Mol. A variant tupe
Aib 46.26 — — — −135.7
β-Res −72.79 72.9 — — 83.78
Mol.B
Aib −47.38 — — — 130.2
β-Res 84.64 69.14 — — −193.71
αγ-turns (C12)
Boc-Aib-Gpn-Aib-Gpn-OMe/Ananda et al. (2005) αγ Aib 1 −59.8 — — — −37.8 —
Gpn 2 −126.8 52.1 63.8 −107.9
Boc-Aib-Gpn-Aib-Gpn-OMe/Ananda et al. (2005) γα Gpn 2 −126.8 52.1 63.8 — −107.9 —
Aib 3 −51.5 — — — −48.8
Boc-Leu-Aib-Val-βGly-γAbu-Leu-Aib-Val-OMe/Karle et al. (1997) γα γAbu5 −108 58 66 — −169 —
Leu 6 −86 — — — −18
Boc-Leu-Aib-Val-βGly-γAbu-Leu-Aib-Val-Ala-Leu-Aib-OMe/Karle et al. (1997) γα γAbu5 −121 62 67 — −169 —
Leu 6 −57 — — — −37
Boc-Val-Ile-γResZ-Val-Ile-OMe/Wolfe et al. (1998) γα γ-ResZ −101.2 65.2 62.6 — −140.5
Leu 90.0 — — — −28.5 —
Boc-γ-Abu-Aib-Ala-Aib-OMe/Maji et al. (2002) γα γAbu1 92.7 −69.7 −65.8 — 155.7 —
Leu 2 58.4 — — — 26.1
Boc-γ-ResX-DPro-Gly-γ-ResY-OMe/Hagihara et al. (1992) γα MolA
γ-ResX −98.7 66.2 66.63 — −149.3
Pro −64.2 — — — −14.2 —
MolB
γ-ResX −100.8 58.8 65.11 — −160.1 —
Pro −69.9 — — — −14.8
Boc-γ-Abu-Aib-Ala-OMe/Maji et al. (2002) γα MolA
γAbu1 −109.2 65.2 62.6 — −140.4
Aib2 −54.5 — — — −37.0 —
MolB
γAbu1 107.5 −62.3 −65.1 — 138.4 —
Aib2 58.35 — — — 36.36
ββ-turns (C12)
Boc-(trans-ACPC)8-CO2CH2Ph/Appella et al. (1999c) ββd trans ACPC 97.9 96.4 — — 106.3 —
trans ACPC 97.9 96.4 — — 106.3
Boc-(trans ACPC-trans ACPC-Phe)2 OMe/Schmitt et al. (2006) ββ trans ACPC1 −122.5 77.9 — — −112.0 —
trans ACPC2 −67.5 105.8 — — −129.8
Boc-(trans ACPC- trans ACPC-Phe)2OMe/Schmitt et al. (2006) ββ trans ACPC4 −112.5 74.9 — — −78.8 —
trans ACPC5 −92.2 90.1 — — −98.9
Piv-β-Res A-Nip1-Nip2-β-Res B-NHMe/Chung et al. (1998) ββ Nip 1 115.7 −175.2 — — 81.8 —
Nip 2 −117.4 −176.6 — −71.2
Boc-B-Ala-(R)-Nip-(S)- Nip-β-Ala-NHMe/Chung et al. (2000) ββe Nip 1 98.8 −177.4 — — 81.7 —
Nip 2 −121.8 179.3 — −59.4
βγ-turns (C13)
Boc-Leu-Aib-Val-βGly-γAbu-Leu-Aib-Val-OMe/Karle et al. (1997) βγ βGly4 −103 78 — — −107 —
γAbu5 −121 63 57 — −121
αδ-turns (C13)
Boc-Leu-Val-Val-DPro-δAva-Leu-Val-Val-OMe/Rai et al. (in press) αδ DPro 4 64.1 — — — −156.9 —
δAva5 −126.8 53.2 61.7 166.5 76.9
γγ-turns (C14)
Boc-γ-Res A-γ-Res B-NHMe/Brenner & Seebach (2001) γγ γ-Res1 157.9 −167 67.8 — −113.6 —
γ-Res2 −121.8 59.5 −177.8 — 149.6
Ac-γ-Res A-γ-Res B-NHMe/Brenner & Seebach (2001) γγe γ-Res1 148.1 −169.4 73.4 — −112.6 —
γ-Res2 −119.9 60.4 176.7 — 147.1
Boc-(γ-ResC-γ-ResD-)2OBz/Seebach et al. (2001a) γγe γ-Res3 132.4 −69.9 −56.9 — 138.9 —
γ-Res4 153.5 −70.4 −56.3 — 124.9
a

Torsion angle values for Aib residue in the αβ-turn is averaged over Aib residues 1, 3 and 5 and in the βα turn is averaged over the Aib residues 3, 5 and 7. Torsion angles of trans ACPC residue is averaged over residues 2, 4 and 6.

b

Torsion angle values for trans ACPC is averaged over residues 1 and 4, while Aib is averaged over residues 2 and 5.

c

Achiral peptide.

d

Torsion angles averaged over the 7 trans ACPC residues of the peptide from the N-terminus. C-terminal residue has been excluded as the helix frays at the C-terminus.

e

Torsion angles averaged over the residues in the two independent molecules in the crystal.