The Important Roles of Water in Protein Folding: an Approach by Single Molecule Force Spectroscopy

Bo Cheng; Shu-Xun Cui

doi:10.1007/s10118-018-2082-2

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The Important Roles of Water in Protein Folding: an Approach by Single Molecule Force Spectroscopy

ARTICLES | Updated：2021-02-18

- The Important Roles of Water in Protein Folding: an Approach by Single Molecule Force Spectroscopy
- Chinese Journal of Polymer Science Vol. 36, Issue 3, Pages: 379-384(2018)
- Affiliations：
  
  a.School of Mechanical Engineering, North University of China, Taiyuan 030051, China
  b.Key Lab of Advanced Technologies of Materials, Ministry of Education of China, Southwest Jiaotong University, Chengdu 610031, China
- Author bio：
  
  Shu-Xun Cui, E-mail cuishuxun@swjtu.edu.cn
- Funds：
- DOI：10.1007/s10118-018-2082-2
  CLC：
- Received：23 September 2017，
  
  Accepted：02 November 2017，
  
  Online First：07 December 2017，
  
  Published：05 March 2018
- Accepted：
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Bo Cheng, Shu-Xun Cui. The Important Roles of Water in Protein Folding: an Approach by Single Molecule Force Spectroscopy[J]. Chinese Journal of Polymer Science, 2018, 36(3): 379-384.
DOI：

Bo Cheng, Shu-Xun Cui. The Important Roles of Water in Protein Folding: an Approach by Single Molecule Force Spectroscopy[J]. Chinese Journal of Polymer Science, 2018, 36(3): 379-384. DOI： 10.1007/s10118-018-2082-2.

摘要

Abstract

The single-chain elasticity of a completely unfolded protein ((I27)

modules of human cardiac titin) is studied in different liquid environments by the atomic force microscopy (AFM)-based single molecule force spectroscopy (SMFS). The experimental results show that there is a clear deviation between the force curves obtained in the aqueous and nonaqueous environments. Such a deviation can be attributed to the additional energy consumed by the rearrangement of the bound water molecules around the chain of the completely unfolded (I27)

chain upon stretching in aqueous solution

which is very similar to the partial dehydration process from a denatured/unfolded to a native/folded protein. Through the analysis of the free energy changes involved in protein folding

we conclude that it is due to the weak disturbance of water molecules and the special backbone structures of proteins that the self-assembly of proteins can be achieved in physiological conditions. We speculate that water is likely to be an important criterion for the selection of self-assembling macromolecules in the prebiotic chemical evolution.

关键词

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references

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