Extent of Helical Induction Caused by Introducing α-Aminoisobutyric Acid into an Oligovaline Sequence | Zendy

Genichiro Tsuji | Zendy; Takashi Misawa | Zendy; Mitsunobu Doi | Zendy; Yosuke Demizu | Zendy

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Extent of Helical Induction Caused by Introducing α-Aminoisobutyric Acid into an Oligovaline Sequence

Author(s) -

Genichiro Tsuji,

Takashi Misawa,

Mitsunobu Doi,

Yosuke Demizu

Publication year - 2018

Publication title -

acs omega

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.779

H-Index - 40

ISSN - 2470-1343

DOI - 10.1021/acsomega.8b01030

Subject(s) - aminoisobutyric acid , valine , sequence (biology) , peptide , helix (gastropod) , crystallography , chemistry , stereochemistry , amino acid , peptide sequence , solid state , biochemistry , biology , gene , ecology , snail

The preferred conformations of a dodecapeptide composed of l-valine (l-Val) and α-aminoisobutyric acid (Aib) residues, Boc-(l-Val-l-Val-Aib) 4 -OMe ( 3 ), were analyzed in solution and in the crystalline state. Peptide 3 predominantly folded into a mixture of α- and 3 10 -( P ) helical structures in solution and a ( P ) α helix in the crystalline state.

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