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Crystal structure of L-Pro-L-Leu-Aib-Aib-L-Glu-L-Valol, the C-terminal hexapeptide fragment of trichotoxin

✍ Scribed by Michael Kokkinidis; David W. Banner; Demetrius Tsernoglou; Hans Brückner

Book ID
117056862
Publisher
Elsevier Science
Year
1986
Tongue
English
Weight
331 KB
Volume
139
Category
Article
ISSN
0006-291X

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Crystal structure of Boc-Leu-Aib-Pro-Val
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Boc-L-Leu-Aib-Pro-Val-AibAibGlu(OBz1)-Gln-Phl (Boc = t-butyloxycarbonyl, Aib = a-aminoisobutyric acid, Bzl = benzyl, Phl = phenylalaninol), C59H,Nlo0,,, the protected C-terminal nonapeptide with the sequence 12-20 of alamethicin, crystallize: in the orthorhombic space group P2,2121 with a = 15.666,

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## Abstract The x‐ray structure of Boc‐L‐Ala‐Aib‐Ala‐Aib‐Ala‐Glu(OBzl)‐Ala‐Aib‐Ala‐Aib‐Ala‐OMe(I) represents the first α‐helix determined by direct methods. This undecapeptide is a model of the N‐terminus of alamethicin, and it exhibits voltage‐dependent pores in bilayer membranes at a higher volta

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As models of the helical N-terminal part of alamethicin the undecapeptides Boc-L-Ala-[Aib-Ala]2-Glu(0Bzl)-Ala-[Aib-Ala],-OMe (1) and Boc-~-Ala-[Aib-Ala]~-Gly-Ala-[Aib-Ala]~-OMe (2) were synthesized. 1 was examined by X-ray crystallography using direct methods for solution of the phase problem. The u

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Peptide design: Influence of a guest Aib-Pro segment on the stereochemistry of an Oligo-Val sequence—solution conformations and crystal structure of Boc-(Val)2-Aib-Pro-(Val)3-OMe
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## SYNOPSIS T h e peptide Boc-Val-Val-Aib-Pro-Val-Val-Val-OMe has been synthesized t o investigate the effect of introduction of a strong 8-turn promoting guest segment into a n oligopeptide with a tendency t o form extended structures. 'H-nmr studies in solution using analysis of N H group solven

Accommodation of a D-Phe residue into a
Accommodation of a D-Phe residue into a right-handed 310-helix: Structure of Boc-D-Phe-(Aib)4-Gly-L-Leu-(Aib)2-Ome, an analogue of the amino terminal segment of antiamoebins and emerimicins
✍ I. L. Karle; J. L Flippen-Anderson; K. Uma; P. Balaram 📂 Article 📅 1993 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 535 KB

OMe (I), which is an analogue of the N-terminal sequence of antiamoebins and emerimicins, establishes a completely 3,0-helical conformation with seven successive intramolecular 4 + 1 hydrogen bonds. The average, 4,+ values for residues 1-8 are -59" and -32", respectively. Crystal parameters are C47H