Table 3.

Stability changes in proteins and protein domains produced upon proline-to-fluoroproline replacements.^a

protein		number of replaced proline residues		change in the thermodynamic stability			references
				R-Flp	S-Flp	Dfp
barstar		1		↓	↑	≈	[16,127]
tryptophan cage miniprotein		1		↑	↓	not examined	[128]
enhanced green fluorescent protein		10		insoluble	folded, no data	not examined	[117,142]
villin headpiece subdomain		1		↓	≈	not examined	[129]
T. thermohydrosulfuricus lipase		6		↓	↓	not examined	[130–132]
human ubiquitin		3		↑	no production	not examined	[133]
single chain Fv format protein		8		↑	insoluble	not examined	[134]
KlenTag DNA polymerase		32		↓	no production	not examined	[119,135]
thioredoxin A single proline	reduced	1		↑	↑	not examined	[120,143]
	oxidized	1		↓	↓
β2-microglobulin		1		↓	↑	↓	[136]
bacteriophage T4 fibritin C‐terminal domain		2	position 4 position 7	↓ ↑	↑ ↓	not examined	[106]
red fluorescent protein (mRFP1)		12 (11)		↑	insoluble	not examined	[137–138]
Pin1 WW domain		1		↓	↑	not examined	[139]
ribonuclease A		1		not examined	↑	not examined	[140]

^aAs summarized from the thermal stability and other reported data that reflect the stability.