Molecular mechanisms of 33-mer gliadin peptide oligomerisation-Reference-Cited by-同舟云学术

Molecular mechanisms of 33-mer gliadin peptide oligomerisation

Published:2019 Issue:40 Volume:21 Page:22539-22552
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Amundarain María Julia¹²³⁴⁵^ORCID,Herrera María Georgina⁶⁷⁸⁹¹⁰,Zamarreño Fernando¹²³⁴⁵^ORCID,Viso Juan Francisco¹²³⁴⁵,Costabel Marcelo D.¹²³⁴⁵^ORCID,Dodero Verónica I.⁶⁷⁸⁹¹⁰^ORCID

Affiliation:

1. Grupo de Biofísica

2. Instituto de Física del Sur

3. Universidad Nacional del Sur

4. Bahía Blanca

5. Argentina

6. Universität Bielefeld

7. Fakultät für Chemie

8. Organische Chemie

9. 33615 Bielefeld

10. Germany

Abstract

The 33-mer gliadin peptide oligomerizes driven by its non-ionic polar character, flexible PPII secondary structure and stable glutamine H-bonds.

Funder

Alexander von Humboldt-Stiftung

Deutscher Akademischer Austauschdienst

Consejo Nacional de Investigaciones Científicas y Técnicas

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2019/CP/C9CP02338K

Reference74 articles.

1. Translational Chemistry Meets Gluten-Related Disorders

2. Spectrum of gluten-related disorders: consensus on new nomenclature and classification

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4. Structural Basis for Gluten Intolerance in Celiac Sprue

5. Coeliac disease

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