Peptide hairpin nucleation with the obligatory Type I' beta-turn Aib-DPro segment.
نویسندگان
چکیده
The alpha-aminoisobutyric acid-D-proline (Aib-(D)Pro) dipeptide is an obligatory Type I' beta-turn forming segment that nucleates hairpin formation.
منابع مشابه
De novo protein design: crystallographic characterization of a synthetic peptide containing independent helical and hairpin domains.
The Meccano (or Lego) set approach to synthetic protein design envisages covalent assembly of prefabricated units of peptide secondary structure. Stereochemical control over peptide folding is achieved by incorporation of conformationally constrained residues like alpha-aminoisobutyric acid (Aib) or DPro that nucleate helical and beta-hairpin structures, respectively. The generation of a synthe...
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The competing effects of a disulfide bridge and an alpha-aminoisobutyryl residue (Aib) in determining the conformation of a hexapeptide have been investigated, by comparing the cyclic disulfide [sequence: see text] and the acylic peptide Boc-Cys (SBzl)-Val-Aib-Ala-Leu-Cys (SBzl)-NHMe (2). Previously published nmr and crystallographic studies [R. Kishore, S. Raghothama, and P. Balaram (1987) Bio...
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The design of a peptide that contains two distinct elements of secondary structure, helix and beta-hairpin, is described. Two designed 17-residue peptides: Boc-Val-Ala-Leu-Aib-Val-Ala-Leu-Gly-Gly-Leu-Phe-Val-D-Pro-Gly-Leu-Phe-Val-OMe (I) and Boc-Leu-Aib-Val-Ala-Leu-Aib-Val-Gly-Gly-Leu-Val-Val-D-Pro-Gly-Leu-Val-Val-OMe (II) have been conformationally characterized by NMR spectroscopy. Peptides I...
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ورودعنوان ژورنال:
- Organic & biomolecular chemistry
دوره 8 14 شماره
صفحات -
تاریخ انتشار 2010