Direct observation of protein structural transitions through entire amyloid aggregation processes in water using 2D-IR spectroscopy-Reference-Cited by-同舟云学术

Direct observation of protein structural transitions through entire amyloid aggregation processes in water using 2D-IR spectroscopy

Published:2022 Issue:16 Volume:13 Page:4482-4489
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Chun So Yeon¹²,Son Myung Kook²³⁴,Park Chae Ri²³⁴,Lim Chaiho¹²,Kim Hugh I.²³⁴^ORCID,Kwak Kyungwon¹²^ORCID,Cho Minhaeng¹²

Affiliation:

1. Center for Molecular Spectroscopy and Dynamics, Institute for Basic Science (IBS), Seoul 02841, Republic of Korea

2. Department of Chemistry, Korea University, Seoul 02841, Republic of Korea

3. Center for Proteogenome Research, Korea University, Seoul 02841, Republic of Korea

4. Single Cell Analysis Laboratory, Korea University, Seoul 02841, Republic of Korea

Abstract

This study aims to understand the structural transition dynamics of INS during amyloid aggregation in H2O using 2D-IR spectroscopy. The results show that distinct fibrillations in D2O and H2O originated from different quaternary structures of INS.

Funder

Institute for Basic Science

Ministry of Science and ICT, South Korea

Ministry of Education

Ministry of Science, ICT and Future Planning

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2022/SC/D1SC06047C

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