Table 1 Thermodynamic stability of mutant αIIbβ3 TM complexes.
From: Structural and thermodynamic basis of proline-induced transmembrane complex stabilization
Peptides | KXYa | ΔH° [kcal/mol] | ΤΔS° [kcal/mol] | ΔG° [kcal/mol] | ΔΔG°,′b [kcal/mol] |
|---|---|---|---|---|---|
αIIb + β3 c | 3250 ± 60 | −16.0 ± 0.1 | −11.1 ± 0.1 | −4.84 ± 0.01 | — |
αIIb + β3(A711P) | 12700 ± 200 | −16.9 ± 0.1 | −11.2 ± 0.1 | −5.66 ± 0.01 | — |
αIIb(G972A) + β3 | 1080 ± 30 | −14.2 ± 0.2 | −10.1 ± 0.2 | −4.18 ± 0.01 | — |
αIIb(G972A) + β3(A711P) | 5500 ± 300 | −16.2 ± 0.3 | −11.0 ± 0.3 | −5.16 ± 0.03 | 0.16 ± 0.03 |
αIIb + β3(L712A) | 1900 ± 50 | −12.0 ± 0.1 | −7.4 ± 0.1 | −4.52 ± 0.01 | — |
αIIb + β3(A711P/L712A) | 4200 ± 100 | −12.8 ± 0.1 | −7.8 ± 0.1 | −5.00 ± 0.01 | −0.34 ± 0.01 |
αIIb + β3(W715Y) | 1300 ± 40 | −14.2 ± 0.2 | −9.9 ± 0.2 | −4.30 ± 0.02 | — |
αIIb + β3(A711P/W715Y) | 2200 ± 100 | −14.4 ± 0.4 | −9.8 ± 0.4 | −4.61 ± 0.03 | −0.51 ± 0.04 |
αIIb(R995A) + β3 c | 250 ± 70 | −15 ± 4 | −12 ± 4 | −3.3 ± 0.2 | — |
αIIb(R995A) + β3(A711P) | 4000 ± 300 | −5.6 ± 0.2 | −0.59 ± 0.2 | −4.98 ± 0.04 | 0.8 ± 0.2 |
