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https://doi.org/10.1002/anie.201700411
DC Field | Value | |
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dc.title | Elasticity of the Transition State Leading to an Unexpected Mechanical Stabilization of Titin Immunoglobulin Domains | |
dc.contributor.author | Yuan Guohua | |
dc.contributor.author | LE SHIMIN | |
dc.contributor.author | YAO MINGXI | |
dc.contributor.author | Qian hui | |
dc.contributor.author | Zhou Xin | |
dc.contributor.author | YAN JIE | |
dc.contributor.author | CHEN HU | |
dc.date.accessioned | 2020-07-01T08:25:36Z | |
dc.date.available | 2020-07-01T08:25:36Z | |
dc.date.issued | 2017-05-08 | |
dc.identifier.citation | Yuan Guohua, LE SHIMIN, YAO MINGXI, Qian hui, Zhou Xin, YAN JIE, CHEN HU (2017-05-08). Elasticity of the Transition State Leading to an Unexpected Mechanical Stabilization of Titin Immunoglobulin Domains. Angewandte Chemie (International ed. in English) 129 (20) : 5582-5585. ScholarBank@NUS Repository. https://doi.org/10.1002/anie.201700411 | |
dc.identifier.issn | 1433-7851 | |
dc.identifier.issn | 1521-3773 | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/170838 | |
dc.description.abstract | The giant protein titin plays a critical role in regulating the passive elasticity of muscles, mainly through the stochastic unfolding and refolding of its numerous immunoglobulin domains in the I‐band of sarcomeres. The unfolding dynamics of titin immunoglobulin domains at a force range greater than 100 pN has been studied by atomic force microscopy, while that at smaller physiological forces has not been measured before. By using magnetic tweezers, it is found that the titin I27 domain unfolds in a surprising non‐monotonic force‐dependent manner at forces smaller than 100 pN, with the slowest unfolding rate occurring around 22 pN. We further demonstrate that a model with single unfolding pathway taking into account the elasticity of the transition state can reproduce the experimental results. These results provide important novel insights into the regulation mechanism of the passive elasticity of muscle tissues. | |
dc.language.iso | en | |
dc.publisher | Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim | |
dc.subject | Bell's model | |
dc.subject | catch bonds | |
dc.subject | Protein Unfolding | |
dc.subject | Titin | |
dc.subject | Transition states | |
dc.type | Article | |
dc.contributor.department | PHYSICS | |
dc.contributor.department | MECHANOBIOLOGY INSTITUTE | |
dc.description.doi | 10.1002/anie.201700411 | |
dc.description.sourcetitle | Angewandte Chemie (International ed. in English) | |
dc.description.volume | 129 | |
dc.description.issue | 20 | |
dc.description.page | 5582-5585 | |
dc.description.coden | ACIEAY | |
dc.published.state | Published | |
dc.grant.id | NRF-NRFI2016-03 | |
dc.grant.id | B16029 | |
dc.grant.id | 2013121005 | |
dc.grant.id | 11474237 | |
dc.grant.id | 11574310 | |
dc.grant.fundingagency | National Research Foundation (NRF), Prime Minister's Office, Singapore | |
dc.grant.fundingagency | Ministry of Education, China | |
dc.grant.fundingagency | Fundamental Research Funds for the Central Universities, China | |
dc.grant.fundingagency | National Nature Science Foundation of China | |
Appears in Collections: | Staff Publications Elements |
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Yuan_et_al-2017-Angewandte_Chemie.pdf | 1.37 MB | Adobe PDF | CLOSED | Published | ||
Accepted-Manuscript-Elasticity of the Transition State Leading to an Unexpected Mechanical Stabilization of Titin Immunoglobulin Domains.pdf | 1.64 MB | Adobe PDF | OPEN | Post-print | View/Download |
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