Effect of the geometry of confining media on the stability and folding rate of α-helix proteins-Reference-Cited by-同舟云学术

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Effect of the geometry of confining media on the stability and folding rate of α-helix proteins

Published:2018-05-21 Issue:19 Volume:148 Page:194305
ISSN:0021-9606
Container-title:The Journal of Chemical Physics
language:en
Short-container-title:The Journal of Chemical Physics

Author:

Wang Congyue¹,Piroozan Nariman¹,Javidpour Leili²³,Sahimi Muhammad¹

Affiliation:

1. Mork Family Department of Chemical Engineering and Materials Science, University of Southern California, Los Angeles, California 90089-1211, USA

2. Departments of Energy Engineering and Physics, Amirkabir University of Technology, Tehran 15875-4413, Iran

3. School of Physics, Institute for Research in Fundamental Sciences (IPM), Tehran 19395-5531, Iran

Publisher

AIP Publishing

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://aip.scitation.org/doi/pdf/10.1063/1.5020841

Reference74 articles.

1. Confinement in nanopores can destabilize α-helix folding proteins and stabilize the β structures

2. X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation.

3. Amyloid diseases: Abnormal protein aggregation in neurodegeneration

4. Acceleration of oligomerization, not fibrillization, is a shared property of both alpha -synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy

5. Review: Model Peptides and the Physicochemical Approach to β-Amyloids

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1. Ribosome Tunnel Environment Drives the Formation of α-Helix during Cotranslational Folding;Journal of Chemical Information and Modeling;2024-08-16

2. Molecular Dynamics Study of Structure, Folding, and Aggregation of Poly-PR and Poly-GR Proteins;Biophysical Journal;2021-01

3. Common mechanism of thermostability in small α‐ and β‐proteins studied by molecular dynamics;Proteins: Structure, Function, and Bioinformatics;2020-05-19

4. Molecular dynamics study of structure, folding, and aggregation of poly-glycine-alanine (Poly-GA);The Journal of Chemical Physics;2019-04-14

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