Chemical crosslinking with disuccinimidyl tartrate defines the relative positions of the two antiparallel coiled coils of the desmin protofilament unit.
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 alpha-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.
Geisler
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Max Planck Institute for Biophysical Chemistry, Department of Biochemistry, Goettingen, Germany.
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D003432:Cross-Linking Reagents / Q000494:pharmacology*; D003893:Desmin / Q000737:chemistry*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013388:Succinimides / Q000494:pharmacology*
D003432:Cross-Linking Reagents; D003893:Desmin; D013388:Succinimides; C018052:disuccinimidyl tartarate