Conformational Heterogeneity of a Tripeptide in the Solid State and in Solution: Characterization of a g-Turn Containing Incipient Hairpin in Solution

Maji, S. K. ; Haldar, D. ; Banerjee, A. ; Mukhopadhyay, Ch. ; Banerjee, A. (2003) Conformational Heterogeneity of a Tripeptide in the Solid State and in Solution: Characterization of a g-Turn Containing Incipient Hairpin in Solution Journal of Structural Chemistry, 44 (5). pp. 790-795. ISSN 0022-4766

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Official URL: http://doi.org/10.1023/B:JORY.0000029816.31278.7b

Related URL: http://dx.doi.org/10.1023/B:JORY.0000029816.31278.7b

Abstract

A terminally blocked tripeptide Boc-β-Ala-Aib-β-Ala-OMe 1 with noncoded amino acids forms a novel type of hairpin structure containing a γ-turn instead of a conventional β-turn in the central loop region in solution. This new type structural motif was characterized by NMR and restraint molecular dynamics simulation study. In the solid state peptide 1 adopts an extended backbone conformation and self-assembles to form supramolecular β-sheet.

Item Type:Article
Source:Copyright of this article belongs to Springer Nature Switzerland AG
Keywords:β-Ala;Aib;γ-turn;incipient hairpin;solution structure
ID Code:126613
Deposited On:31 Oct 2022 04:27
Last Modified:31 Oct 2022 04:27

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