Chemical crosslinking with disuccinimidyl tartrate defines the relative positions of the two antiparallel coiled coils of the desmin protofilament unit | Zendy

Geisler Norbert | Zendy

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Chemical crosslinking with disuccinimidyl tartrate defines the relative positions of the two antiparallel coiled coils of the desmin protofilament unit

Author(s) -

Geisler Norbert

Publication year - 1993

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(93)81449-a

Subject(s) - antiparallel (mathematics) , desmin , coiled coil , tartrate , chemistry , protein filament , ethylene glycol , intermediate filament , crystallography , biophysics , biochemistry , biology , cytoskeleton , physics , organic chemistry , vimentin , immunohistochemistry , quantum mechanics , magnetic field , cell , immunology

Filaments formed by desmin, the myogenic intermediate filament protein, were crosslinked with the lysine specific crosslinker DST (disuccinimidyl tartrate; 0.64 nm span) and three DST crosslinked peptides were characterized. Two correspond to crosslinks previously obtained with the longer crosslinker EGS (ethylene glycol bis(succinimidylsuccinate), 1.61 nm span) which defined the antiparallel on‐stagger relationship of neighbouring coiled coils. The two DST crosslinks now provide the relative positions of the coiled coils within a limit of about 9 α‐helical residues. The third DST crosslink most likely connecting two helices of a single coiled coil gives a direct measure of the distance spanned in DST crosslinks.

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