Kinetics Study on the HIV-1 Ectodomain Protein Quaternary Structure Formation Reveals Coupling of Chain Folding and Self-Assembly in the Refolding Cascade-Reference-Cited by-同舟云学术

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Kinetics Study on the HIV-1 Ectodomain Protein Quaternary Structure Formation Reveals Coupling of Chain Folding and Self-Assembly in the Refolding Cascade

Published:2014-11-03 Issue:45 Volume:118 Page:12827-12836
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Cheng Shu-Fang¹,Sung Tai-Ching²,Chang Chung-Chieh¹,Chou Mei-Ju¹,Chiang Yun-Wei²,Chang Ding-Kwo¹

Affiliation:

1. Institute of Chemistry, Academia Sinica, Taipei, Taiwan, Republic of China 11529

2. Department of Chemistry and Frontier Research Center on Fundamental and Applied Sciences of Matters, National Tsing Hua University, Hsinchu, Taiwan, Republic of China 30013

Funder

National Science Council Taiwan

Academia Sinica

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp508360k

Reference48 articles.

1. Capture of an early fusion-active conformation of HIV-1 gp41

2. Emergence of a Drug-Dependent Human Immunodeficiency Virus Type 1 Variant during Therapy with the T20 Fusion Inhibitor

3. A Kinetic Approach to Determining the Conformational Stability of a Protein That Dimerizes after Folding

4. Extremely Fast Folding of a Very Stable Leucine Zipper with a Strengthened Hydrophobic Core and Lacking Electrostatic Interactions between Helices

5. Three-dimensional solution structure of the 44kDa ectodomain of SIV gp41

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