Skip to main content
. Author manuscript; available in PMC: 2019 Jun 21.
Published in final edited form as: J Phys Chem B. 2018 Mar 6;122(10):2725–2736. doi: 10.1021/acs.jpcb.7b11596

Table 1.

Primary sequences, number of residues, residue averaged Kyte-Doolittle hydrophobicities (hyd) and coacervation temperatures (Tc) of constituent modules and minielastins 1–4.

Protein Sequence #aa hyd Tc(°C)a
20’ (VPGVGG)5 30 0.9 ND
24’ (APGVGV)7 42 1.3 ND
2123 EAQA5KA2KYGVGTPA5KA3KAAQFG 33 0.2 NC
X’ DA5KA2KF 11 0.4 NC
1 20’−2123–24’−2123–24’ 182 0.8 52
2 20’−20’−2123–24’−2123–24’−24’ 254 0.9 32
3 20’-X’−24’-X’−24’ 138 1.0 44
4 24’-X’−24’-X’−24’-X’−24’ 203 1.1 36
a

Tc values were determined spectrophotometrically by the onset of turbidity at 440 nm under standard conditions: 25 μM protein in pH 7, 50 mM Tris with 1.5 M NaCl and 1 mM CaCl2. For easy detection, constructs 1–4 contain tryptophan residues at the N- and C- termini.