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


ABSTRACT: The preferred conformations of a dodecapeptide composed of l-valine (l-Val) and ?-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 ?- and 310-(P) helical structures in solution and a (P) ? helix in the crystalline state.

SUBMITTER: Tsuji G 

PROVIDER: S-EPMC6644412 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature

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

Tsuji Genichiro G   Misawa Takashi T   Doi Mitsunobu M   Demizu Yosuke Y  

ACS omega 20180614 6


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

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