The single-chain elasticity of a completely unfolded protein （027）8, modules of human cardiac titin） is studied in different liquid environments by the atomic force microscopy （AFM）-based single molecule force sp...The single-chain elasticity of a completely unfolded protein （027）8, 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）s 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.展开更多
In this work,the single-chain elasticity of polyformaldehyde(POM)is studied,for the first time,by employing atomic force microscopy(AFM)-based single molecule force spectroscopy(SMFS).We find that the single-chain ela...In this work,the single-chain elasticity of polyformaldehyde(POM)is studied,for the first time,by employing atomic force microscopy(AFM)-based single molecule force spectroscopy(SMFS).We find that the single-chain elasticity of POM in a nonpolar organic solvent(nonane)can be described well by a theoretical model(QM-FRC model),when the rotating unit length is 0.144 nm(C―O bond length).After comparison,POM is more flexible than polystyrene(a typical polymer with C―C backbone)at the single-chain level,which is reasonable since the C―O bond has a lower rotation barrier than C―C bond.This result indicates that the flexibility of a polymer chain can be tuned by the C―O bond proportion in backbone,which casts new light on the rational design of new synthetic polymers in the future.展开更多
基金financially supported by the National Natural Science Foundation of China(Nos.21574106 and 21604074)the Sichuan Province Youth Science and Technology Innovation Team(Nos.2016TD0026 and 2017JQ0009)
文摘The single-chain elasticity of a completely unfolded protein （027）8, 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）s 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.
基金the National Natural Science Foundation of China(No.21774102).
文摘In this work,the single-chain elasticity of polyformaldehyde(POM)is studied,for the first time,by employing atomic force microscopy(AFM)-based single molecule force spectroscopy(SMFS).We find that the single-chain elasticity of POM in a nonpolar organic solvent(nonane)can be described well by a theoretical model(QM-FRC model),when the rotating unit length is 0.144 nm(C―O bond length).After comparison,POM is more flexible than polystyrene(a typical polymer with C―C backbone)at the single-chain level,which is reasonable since the C―O bond has a lower rotation barrier than C―C bond.This result indicates that the flexibility of a polymer chain can be tuned by the C―O bond proportion in backbone,which casts new light on the rational design of new synthetic polymers in the future.
