Engineering covalent loops in proteins can serve as an on/off switch to regulate threaded topologies-Reference-Cited by-同舟云学术

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Engineering covalent loops in proteins can serve as an on/off switch to regulate threaded topologies

Published:2015-08-20 Issue:35 Volume:27 Page:354107
ISSN:0953-8984
Container-title:Journal of Physics: Condensed Matter
language:
Short-container-title:J. Phys.: Condens. Matter

Author:

Haglund Ellinor

Funder

Division of Physics

Division of Molecular and Cellular Biosciences

National Science Foundation-Directorate for Mathematical and Physical Sciences-Division of Physics

Publisher

IOP Publishing

Subject

Condensed Matter Physics,General Materials Science

Link

http://stacks.iop.org/0953-8984/27/i=35/a=354107/pdf

Reference61 articles.

1. Characterization of a Helical Protein Designed from First Principles

2. De novo proteins from designed combinatorial libraries

3. The packing of α-helices: simple coiled-coils

4. A four-helical super-secondary structure

5. Structural and functional diversity in 4-α-helical proteins

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1. Topology in soft and biological matter;Physics Reports;2024-07

2. Exploring the folding landscape of leptin: Insights into threading pathways;Journal of Structural Biology;2024-03

3. Topological Reaction Coordinate Captures the Folding Transition State Ensemble in a Pierced Lasso Protein;The Journal of Physical Chemistry B;2023-12-20

4. Lasso Proteins—Unifying Cysteine Knots and Miniproteins;Polymers;2021-11-18

5. Topological Twists in Nature;Trends in Biochemical Sciences;2021-06

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