Common folding processes of mini-proteins: Partial formations of secondary structures initiate the immediate protein folding-Reference-Cited by-同舟云学术

Common folding processes of mini-proteins: Partial formations of secondary structures initiate the immediate protein folding

Published:2017-02-13 Issue:11 Volume:38 Page:790-797
ISSN:0192-8651
Container-title:Journal of Computational Chemistry
language:en
Short-container-title:J. Comput. Chem.

Author:

Harada Ryuhei¹^ORCID,Takano Yu²,Shigeta Yasuteru¹

Affiliation:

1. Center for Computational Sciences, University of Tsukuba; 1-1-1 Tennodai Tsukuba Ibaraki 305-8577 Japan

2. Department of Biomedical Information Sciences; Graduate School of Information Sciences, Hiroshima City University; 3-4-1 Ozuka-Higashi, Asa-Minami-Ku Hiroshima 731-3194 Japan

Funder

Japan Society for the Promotion of Science

KAKENHI Grant-in-Aid for Young Scientists (A)

Scientific Research of the Innovative Areas “Dynamic Ordering and Biofunction”

“Photosynergetics”

“3D Active-Site Science”

Publisher

Wiley

Subject

Computational Mathematics,General Chemistry

Reference58 articles.

1. Real-Time NMR Studies of Protein Folding

2. In vitro aging of ß-amyloid protein causes peptide aggregation and neurotoxicity

3. Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease

4. Molecular chaperones in protein folding and proteostasis

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