Parallel packing of alpha-helices in crystals of Boc-Trp-Ile-Ala-Aib-Ile-Val-Aib-Leu-Aib-Pro-Ala-Aib-Pro-Aib-Pro-Phe-OMe·4H<sub>2</sub>O·2CH<sub>3</sub>OH

Flippen-Anderson, J.; Sukumar, M.; Balaram, P.

doi:10.1107/s0108767387084149

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“…The largest difference between the backbones in B and C occurs with a greater helix distortion in B than C helix at the penultimate residue where 4 = -150" and -96", respectively. In helices ending with an Aib residue, there often are helix distortions or reversals at the penultimate residue (see, for example, Karle et al, 1986Karle et al, , 1990a, and these appear to be independent of helix length. If residues 9 and 10 are omitted, the average values for 4 and $ in B, -60.2' and -26.7", respectively, are quite similar to those in C.…”

Section: Resultsmentioning

confidence: 99%

Facile transition between 3₁₀‐ and α‐helix: Structures of 8‐, 9‐, and 10‐residue peptides containing the ‐(Leu‐Aib‐Ala)₂‐Phe‐Aib‐fragment

Karle¹,

Flippen‐Anderson²,

Gurunath³

et al. 1994

Protein Science

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A structural transition from a 3,0-helix to an a-helix has been characterized at high resolution for an octapeptide begins as a 3,,-helix and abruptly changes to an a-helix at carbonyl 0(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 though the last 8 residues have the same sequence in all 3 peptides. The average q5,$ angles in the decapeptide are -58", -28" for residues 1-3 and -63", -41 O 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 310-to a-helix transition with the amide I band appearing at 1,656-1,657 cm" in the 9-and 10-residue peptides, whereas in shorter sequences the band is observed at 1,667 cm-l.

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Section: Resultsmentioning

confidence: 99%

Facile transition between 3₁₀‐ and α‐helix: Structures of 8‐, 9‐, and 10‐residue peptides containing the ‐(Leu‐Aib‐Ala)₂‐Phe‐Aib‐fragment

Karle¹,

Flippen‐Anderson²,

Gurunath³

et al. 1994

Protein Science

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Parallel packing of alpha-helices in crystals of Boc-Trp-Ile-Ala-Aib-Ile-Val-Aib-Leu-Aib-Pro-Ala-Aib-Pro-Aib-Pro-Phe-OMe·4H₂O·2CH₃OH

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Facile transition between 3₁₀‐ and α‐helix: Structures of 8‐, 9‐, and 10‐residue peptides containing the ‐(Leu‐Aib‐Ala)₂‐Phe‐Aib‐fragment

Facile transition between 3₁₀‐ and α‐helix: Structures of 8‐, 9‐, and 10‐residue peptides containing the ‐(Leu‐Aib‐Ala)₂‐Phe‐Aib‐fragment

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Parallel packing of alpha-helices in crystals of Boc-Trp-Ile-Ala-Aib-Ile-Val-Aib-Leu-Aib-Pro-Ala-Aib-Pro-Aib-Pro-Phe-OMe·4H2O·2CH3OH

Cited by 1 publication

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Facile transition between 310‐ and α‐helix: Structures of 8‐, 9‐, and 10‐residue peptides containing the ‐(Leu‐Aib‐Ala)2‐Phe‐Aib‐fragment

Facile transition between 310‐ and α‐helix: Structures of 8‐, 9‐, and 10‐residue peptides containing the ‐(Leu‐Aib‐Ala)2‐Phe‐Aib‐fragment

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Parallel packing of alpha-helices in crystals of Boc-Trp-Ile-Ala-Aib-Ile-Val-Aib-Leu-Aib-Pro-Ala-Aib-Pro-Aib-Pro-Phe-OMe·4H₂O·2CH₃OH

Facile transition between 3₁₀‐ and α‐helix: Structures of 8‐, 9‐, and 10‐residue peptides containing the ‐(Leu‐Aib‐Ala)₂‐Phe‐Aib‐fragment

Facile transition between 3₁₀‐ and α‐helix: Structures of 8‐, 9‐, and 10‐residue peptides containing the ‐(Leu‐Aib‐Ala)₂‐Phe‐Aib‐fragment