Table I.
ELP Protein Polymers Subjected to Proteolysis
| Label | Amino acid sequence | aPurity (%) | CMT (°C) | bTt,bulk (°C) | cExpected mass (g mol−1) | dObserved mass (g mol−1) |
|---|---|---|---|---|---|---|
| I96 | G(VPGIG)96Y | 97.7 | n.a. | 11.5 | 40,895 | 40,638 ± 25 |
| V96 | G(VPGVG)96Y | 97.3 | n.a. | 31.9 | 39,548 | 39,514 ± 37 |
| S96 | G(VPGSG)96Y | 92.4 | n.a. | 62.6 | 38,391 | 38,220 ± 3 |
| I48S48 | G(VPGIG)48(VPGSG)48Y | 99.4 | 26 | 87.4 | 39,643 | 39,575 ± 28 |
| S48I48 | G(VPGSG)48(VPGIG)48Y | 99.2 | 27 | 75.7 | 39,643 | 39,541 ± 20 |
| V48 | G(VPGVG)48Y | 98.7 | n.a. | 42.4 | 20,024 | 20,009 ± 11 |
a
Polypeptide purity was assessed using SDS-PAGE and subsequent densitometry of copper chloride stained gel.
b
Inverse transition temperatures, Tt, were analyzed using optical density (350 nm) measurements at a polypeptide concentration of 25 μM.
c
Expected mass of polypeptide (Mean ± SD in Da).
d
Data collected using matrix assisted laser desorption ion time of flight mass spectrometry.