Table 1.

List of protein ELP fusions purified in the Chilkoti lab

Fused protein	ELP guest composition	Number of pentapeptides	MW of protein	Tt*	Citation	Comments
Thioredoxin	V	20	11.8	NA	(Meyer et al. 2001)	Hydrophilic. High levels of expression.
	V5:A2:G3	90		54.0	(Trabbic-Carlson et al. 2004b)
Chloramphenicol Acetyl Transferase	V5:A2:G3	90	25.7	38.3	(Trabbic-Carlson et al. 2004b)
Blue Fluorescent Protein	V5:A2:G3	90	26.9	51.1	(Trabbic-Carlson et al. 2004b)
		120		48.2	unpublished
		180		44	unpublished
Green Fluorescent Protein	V5:A2:G3	90	26.9	52	(Trabbic-Carlson et al. 2004b)
WW domain	V5:A2:G3	90	4.7	45.6	unpublished	Unfolded mutant must be fused to the C-terminus.
Tendamistat	V5:A2:G3	90	8	35.6	(Trabbic-Carlson et al. 2004b)	Hydrophobic. Fused to Thioredoxin to solubilize
Calmodulin	V5:A2:G3	60	16.9	NA	(Kim and Chilkoti 2008)	Final resuspension in HEPES to avoid Ca+2 precipitation.
		180		41**
IL1-Ra	V	30	17	32	(Shamji et al. 2007)
	V5:A2:G3	90		34

^*These T_t are for protein ELP fusion concentrations of 25μM in PBS

^**Measured in HEPES buffer in presence of Ca⁺²