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Structure and stability of pertussis toxin studied by in situ atomic force microscopy
Author(s) -
Yang Jie,
Mou Jianxun,
Shao Zhifeng
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80122-3
Subject(s) - pentamer , oligomer , in situ , atomic force microscopy , crystallography , chemistry , mica , protein subunit , protein quaternary structure , materials science , nanotechnology , polymer chemistry , organic chemistry , biochemistry , composite material , gene
Pertussis toxin, both complete and the B‐oligomer, were imaged by atomic force miroscopy (AFM), using specimens prepared by simple surface adsorption on mica without further manipulation. The spatial arrangement of the subunits of the B‐oligomer was clearly resolved, representing the first protein quaternary structure obtained by AFM in situ. The results suggest that the B‐oligomer is a flat pentamer with the two large subunits located next to each other, and the catalytic A‐subunit situated at the center above. We found that the B‐pentamer was structurally stable for temperatures up to 60°C and within the pH range of 4.5–9.5. It is also demonstrated that the AFM was capable of resolving features down to 0.5 nm on the B‐oligomers, indicating its great potential for structural determination.