Please use this identifier to cite or link to this item: https://doi.org/10.1002/anie.201700411
Title: Elasticity of the Transition State Leading to an Unexpected Mechanical Stabilization of Titin Immunoglobulin Domains
Authors: Yuan Guohua
LE SHIMIN 
YAO MINGXI 
Qian hui
Zhou Xin
YAN JIE 
CHEN HU 
Keywords: Bell's model
catch bonds
Protein Unfolding
Titin
Transition states
Issue Date: 8-May-2017
Publisher: Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim
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
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.
Source Title: Angewandte Chemie (International ed. in English)
URI: https://scholarbank.nus.edu.sg/handle/10635/170838
ISSN: 1433-7851
1521-3773
DOI: 10.1002/anie.201700411
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