α‐Synuclein Spontaneously Adopts Stable and Reversible α‐Helical Structure in Water‐Less Environment-Reference-Cited by-同舟云学术

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α‐Synuclein Spontaneously Adopts Stable and Reversible α‐Helical Structure in Water‐Less Environment

Published:2019-10-14 Issue:21 Volume:20 Page:2783-2790
ISSN:1439-4235
Container-title:ChemPhysChem
language:en
Short-container-title:ChemPhysChem

Author:

Mukhopadhyay Anasua¹,Mehra Surabhi²,Kumar Raj¹,Maji Samir K.²,Krishnamoorthy G.³,Sharma Kamendra P.¹^ORCID

Affiliation:

1. Department of ChemistryIndian Institute of Technology Bombay Mumbai- 400076 INDIA

2. Department of Biosciences and BioengineeringIndian Institute of Technology Bombay Mumbai- 400076 INDIA

3. Department of BiotechnologyAnna University Chennai- 600025 INDIA

Funder

Industrial Research and Consultancy Centre

Indian Institute of Technology Bombay

Publisher

Wiley

Subject

Physical and Theoretical Chemistry,Atomic and Molecular Physics, and Optics

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/cphc.201900868

Reference48 articles.

1. Why are ?natively unfolded? proteins unstructured under physiologic conditions?

2. Natively unfolded proteins: A point where biology waits for physics

3. The rat brain synucleins; family of proteins transiently associated with neuronal membrane

4. Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal

5. The many faces of α-synuclein: from structure and toxicity to therapeutic target

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2. Molecular simulations explain the exceptional thermal stability, solvent tolerance and solubility of protein–polymer surfactant bioconjugates in ionic liquids;Physical Chemistry Chemical Physics;2022

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4. An atomistic view of solvent-free protein liquids: the case of Lipase A;Physical Chemistry Chemical Physics;2021

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