Participation of non-aminoisobutyric acid (Aib) residues in the 310 helical conformation of Aib-rich foldamers: a solid state study-Reference-Cited by-同舟云学术

Participation of non-aminoisobutyric acid (Aib) residues in the 310 helical conformation of Aib-rich foldamers: a solid state study

Author:

Pike Sarah J.¹²³⁴,Boddaert Thomas¹²³⁴,Raftery James¹²³⁴,Webb Simon J.¹²³⁴⁵,Clayden Jonathan¹²³⁴

Affiliation:

1. School of Chemistry

2. University of Manchester

3. Manchester

4. UK

5. Manchester Institute of Biotechnology

Abstract

3₁₀ helical conformations that extend over 21 Å result when selected non-Aib terminal and central residues are incorporated into Aib-rich foldamers.

Funder

European Research Council

Biotechnology and Biological Sciences Research Council

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,General Chemistry,Catalysis

Link

Reference94 articles.

1. Peptaibols, ed. C. Toniolo and H. Brückner, Wiley-VCH, Weinheim, 2009

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