Improved free-energy landscape reconstruction of bacteriorhodopsin highlights local variations in unfolding energy-Reference-Cited by-同舟云学术

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Improved free-energy landscape reconstruction of bacteriorhodopsin highlights local variations in unfolding energy

Published:2018-03-28 Issue:12 Volume:148 Page:123313
ISSN:0021-9606
Container-title:The Journal of Chemical Physics
language:en
Short-container-title:The Journal of Chemical Physics

Author:

Heenan Patrick R.¹²^ORCID,Yu Hao¹,Siewny Matthew G. W.¹²,Perkins Thomas T.¹³^ORCID

Affiliation:

1. JILA, National Institute of Standard and Technology and University of Colorado, Boulder, Colorado 80309, USA

2. Department of Physics, University of Colorado, Boulder, Colorado 80309, USA

3. Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Colorado 80309, USA

Funder

National Science Foundation

DOC | National Institute of Standards and Technology

Publisher

AIP Publishing

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://aip.scitation.org/doi/am-pdf/10.1063/1.5009108

Reference40 articles.

1. The process of folding proteins into membranes: Challenges and progress

2. THEORY OF PROTEIN FOLDING: The Energy Landscape Perspective

3. From Valleys to Ridges: Exploring the Dynamic Energy Landscape of Single Membrane Proteins

4. Reversible Unfolding of Individual Titin Immunoglobulin Domains by AFM

5. Folding-Unfolding Transitions in Single Titin Molecules Characterized with Laser Tweezers

Cited by 18 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Free-energy measuring nanopore device;Physical Review E;2024-02-09

2. Quantifying a light-induced energetic change in bacteriorhodopsin by force spectroscopy;Proceedings of the National Academy of Sciences;2024-02-07

3. Optimal Control of Nonequilibrium Systems through Automatic Differentiation;Physical Review X;2023-11-16

4. Single-Molecule Force Spectroscopy of Membrane Protein Folding;Journal of Molecular Biology;2023-06

5. Untangling the complexity of membrane protein folding;Current Opinion in Structural Biology;2022-02

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