Mechanical response of polyprotein revealed by single-molecule optical tweezers

被引：0
作者：
Li, Shuai [1 ,2 ]
Liu, Haiqing [3 ]
Hu, Chunguang [2 ]
He, Chengzhi [2 ,4 ]
Hu, Huizhu [1 ,5 ]
机构：
[1] Zhejiang Lab, Quantum Sensing Ctr, Hangzhou 310000, Peoples R China
[2] Tianjin Univ, State Key Lab Precis Measuring Technol & Instrume, Tianjin 300072, Peoples R China
[3] Isvis Hangzhou Technol Co Ltd, Hangzhou 310052, Peoples R China
[4] Beijing Univ Chem Technol, Beijing Adv Innovat Ctr Soft Matter Sci & Engn, Beijing 100029, Peoples R China
[5] Zhejiang Univ, Coll Opt Sci & Engn, State Key Lab Modern Opt Instrumentat, Hangzhou 310027, Peoples R China
来源：
APPLIED PHYSICS EXPRESS | 2022年 / 15卷 / 07期
基金：
中国国家自然科学基金;
关键词：
polyprotein; single-molecule force spectroscopy; optical tweezers; mechanical response; energy dissipation; FORCE SPECTROSCOPY; PROTEIN; WORK;
D O I：
10.35848/1882-0786/ac6a40
中图分类号：
O59 [应用物理学];
学科分类号：
摘要：
We researched the mechanical unfolding of protein domains in monomeric protein NuG2 and the tandem polyproteins (NuG2)(8) and (NuG2)(16) using a dual-trap optical tweezers system. By stretching NuG2 and its polyproteins, (NuG2)(8) and (NuG2)(16) at the constant pulling speed of 500 nm s(-1), we achieved the mechanical unfolding force of each domain in these proteins. Besides, we calculated the energy dissipation of NuG2, (NuG2)(8) and (NuG2)(16) by measuring the area enclosed by stretching and relaxation traces. Our results represent a key step towards engineering artificial polyproteins with controllable mechanical force and energy dissipation properties for force-buffering and energy dissipator applications.
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页数：4
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