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Nonmechanical Protein Can Have Significant Mechanical Stability
Author(s) -
Cao Yi,
Lam Canaan,
Wang Meijia,
Li Hongbin
Publication year - 2006
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200502623
Subject(s) - immunoglobulin domain , protein domain , domain (mathematical analysis) , protein g , chemistry , topology (electrical circuits) , antibody , biology , engineering , mathematics , receptor , genetics , biochemistry , electrical engineering , mathematical analysis , gene
The unique topology of the B1 immunoglobulin G (IgG) binding domain of streptococcal protein G (GB1) leads to its remarkable mechanical stability. This nonmechanical protein is shown to be mechanically stable and to unfold at about 180 pN (the force‐extension curves (right) shown demonstrate the mechanical unraveling of each GB1 domain in the polyprotein which is made of direct tandem repeats of GB1 (left)).