Conformational Distribution and α-Helix to β-Sheet Transition of Human Amylin Fragment Dimer-Reference-Cited by-同舟云学术

Conformational Distribution and α-Helix to β-Sheet Transition of Human Amylin Fragment Dimer

Published:2013-12-16 Issue:1 Volume:15 Page:122-131
ISSN:1525-7797
Container-title:Biomacromolecules
language:en
Short-container-title:Biomacromolecules

Author:

Qi Ruxi¹,Luo Yin¹,Ma Buyong²,Nussinov Ruth²³,Wei Guanghong¹

Affiliation:

1. State Key Laboratory of Surface Physics, Key Laboratory for Computational Physical Sciences (MOE), and Department of Physics, Fudan University, Shanghai, China

2. Basic Science Program, Leidos Biomedical Research, Inc., Cancer and Inflammation Program, NCI, Frederick, Maryland 21702, United States

3. Sackler Inst. of Molecular Medicine Department of Human Genetics and Molecular Medicine Sackler School of Medicine, Tel Aviv University, Tel Aviv 69978, Israel

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Polymers and Plastics,Biomaterials,Bioengineering

Link

https://pubs.acs.org/doi/pdf/10.1021/bm401406e

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4. Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients.

5. Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells.

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