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The crystal structure of a 310 helical decapeptide containing α-aminoisobutyric acid

✍ Scribed by A.K. Francis; M. Iqbal; P. Balaram; M. Vijayan

Book ID
115913533
Publisher
Elsevier Science
Year
1983
Tongue
English
Weight
270 KB
Volume
155
Category
Article
ISSN
0014-5793

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Experimental conformational study of two
Experimental conformational study of two peptides containing α-aminoisobutyric acid. Crystal structure of N-acetyl-α-aminoisobutyric acid methylamide
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Some theoretical studies have predicted that the conformational freedom of the cy-aminoisobutyric acid (H-Aib-OH) residue is restricted to the a-helical region of the Ramachandran map. In order to obtain conformational experimental data, two model peptide derivatives, MeCO-Aib-NHMe 1 and Bu'CO-LPro-

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Apolar peptide models for conformational heterogeneity, hydration, and packing of polypeptide helices: Crystal structure of hepta- and octapeptides containing α-aminoisobutyric acid
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## Abstract The crystal structures of two helical peptides Boc‐Val‐Ala‐Leu‐Aib‐Val‐Ala‐Leu‐OMe (VALU‐7) and Boc‐Val‐Ala‐Leu‐Aib‐Val‐Ala‐Leu‐Aib‐OMe (VALU‐8) have been determined to a resolution of 1.0 and 0.9 Å, respectively. Both the seven and eight residue peptides crystallize with two conformers

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## Abstract Boc‐Gly‐L‐Ala‐Aib‐OMe (**1**) crystallizes in the space group __P__2~1~2~1~2~1~ with __a__ = 10.043(3), __b__ = 11.590(5), __c__ = 16.779(1) Å, and __Z__ = 4 (__R__ value for 1859 symmetry independent reflexions: 0.043). On the basis of a 4 → 1 intramolecular hydrogen bond, the tripepti

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Crystal structures of diketopiperazines containing α-aminoisobutyric acid: Cyclo(Aib-Aib) and cyclo(Aib-L-Ile)
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## Abstract The crystal and molecular structures of two α‐aminoisobutyric acid (Aib)‐containing diketopiperazines, cyclo(Aib‐Aib) 1 and cyclo(Aib‐L‐Ile) **2**, are reported. Cyclo(Aib‐Aib) crystallizes in the space group P1 with __a__ = 5.649(3), __b__ = 5.865(2), __c__ = 8.363(1), α = 69.89(6), β