. Author manuscript; available in PMC: 2012 Jun 3.

Published in final edited form as: J Mol Biol. 2011 Apr 2;409(2):202–213. doi: 10.1016/j.jmb.2011.03.049

Table 3.

Effects of cysteine mutations on thermal stability of the dimeric proteins

Mutant protein	Disulfide Linkage		SDS-PAGE^a	Melting Temp (°C)
Mutant protein	Residues	Type	SDS-PAGE^a	Melting Temp (°C)
Cp149.4A	C61-C61	inter	dimer	65
Cp149.5A	none		monomer	63
Cp(−10)149.4A	C(−7)–C61	intra	monomer	51
Cp(−10)149.5A	C61-C61	inter	dimer	60–64
Cp(−10)149.6A	none		monomer	49

SDS-PAGE was performed under non-reducing conditions. The monomer or dimer form is inferred from the apparent molecular weights, ~17 kDa and ~35 kDa respectively, of the proteins. Under reducing conditions all proteins are monomeric.