Morphology and Persistence Length of Amyloid Fibrils Are Correlated to Peptide Molecular Structure-Reference-Cited by-同舟云学术

Morphology and Persistence Length of Amyloid Fibrils Are Correlated to Peptide Molecular Structure

Published:2011-10-24 Issue:45 Volume:133 Page:18030-18033
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

vandenAkker Corianne C.¹,Engel Maarten F. M.¹,Velikov Krassimir P.²³,Bonn Mischa¹⁴,Koenderink Gijsje H.¹

Affiliation:

1. FOM Institute AMOLF, Science Park 104, 1098 XG, Amsterdam, The Netherlands

2. Unilever R&D Vlaardingen, Olivier van Noortlaan 120, 3133 AT Vlaardingen, The Netherlands

3. Soft Condensed Matter, Debye Institute for Nanomaterials Science, Department of Physics and Astronomy, Utrecht University, Princetonplein 5, 3584 CC, Utrecht, The Netherlands

4. Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja206513r

Reference38 articles.

1. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution

2. Amyloids: Not Only Pathological Agents but Also Ordered Nanomaterials

3. Common motifs in protein self-assembly

4. Progress towards a molecular-level structural understanding of amyloid fibrils

5. Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils

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