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Dissociation of intermolecular disulfide bonds in P22 tailspike protein intermediates in the presence of SDS
Author(s) -
Kim Junghwa,
Robinson Anne Skaja
Publication year - 2006
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.062197206
Subject(s) - chemistry , monomer , sodium dodecyl sulfate , folding (dsp implementation) , dissociation (chemistry) , protein folding , disulfide bond , intermolecular force , gel electrophoresis , molecule , biochemistry , organic chemistry , electrical engineering , engineering , polymer
Each chain of the native trimeric P22 tailspike protein has eight cysteines that are reduced and buried in its hydrophobic core. However, disulfide bonds have been observed in the folding pathway and they are believed to play a critical role in the registration of the three chains. Interestingly, in the presence of sodium dodecyl sulfate (SDS) only monomeric chains, rather than disulfide‐linked oligomers, have been observed from a mixture of folding intermediates. Here we show that when the oligomeric folding intermediates were separated from the monomer by native gel electrophoresis, the reduction of intermolecular disulfide bonds did not occur in the subsequent second‐dimension SDS–gel electrophoresis. This result suggests that when tailspike monomer is present in free solution with SDS, the partially unfolded tailspike monomer can facilitate the reduction of disulfide bonds in the tailspike oligomers.