期刊
JOURNAL OF CHEMICAL PHYSICS
卷 130, 期 14, 页码 -出版社
AMER INST PHYSICS
DOI: 10.1063/1.3106761
关键词
biochemistry; free energy; molecular biophysics; proteins
资金
- Ministry of Science and Informatics in Poland [202-204-234]
- Polish committee for UNESCO
Mechanical unfolding of the fourth domain of Distyostelium discoideum filamin (DDFLN4) was studied in detail using the C-alpha-Go model. We show that unfolding pathways of this protein depend on the pulling speed. The agreement between theoretical and experimental results on the sequencing of unfolding events is achieved at low loading rates. The unfolding free energy landscape is also constructed using dependencies of unfolding forces on pulling speeds.
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