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. Author manuscript; available in PMC: 2015 Jun 27.
Published in final edited form as: FEBS Lett. 2014 May 17;588(14):2177–2184. doi: 10.1016/j.febslet.2014.05.006

Table 5.

Δ(ΔG) values for 151 hydrogen bonding variants from 15 proteins for Tyr → Phe, Thr → Val, and Ser → Ala variants.

Hydrogen-bonded Not hydrogen-bonded
Variant number Δ(ΔG)d
(kcal mol−1)
number Δ(ΔG)d
(kcal mol−1)
Tyr → Phe a 35 −1.4 ± 0.9
(−3.6 to 1.2)
17 −0.2 ± 0.4
(−1.2 to 0.5)
Thr → Val b 25 −1.0 ± 1.0
(−3.5 to 1.9)
15 0.0 ± 0.5
(−1.7 to 1.0)
Ser → Ala c 44 −0.8 ± 0.9
(−3.8 to 1.3)
15 0.1 ± 0.4
(−0.8 to 0.5)
a

Fifty-two Tyr → Phe variants from [37].

b

Forty Thr → Val variants from [89].

c

Fifty-nine Ser → Ala variants from [104].

d

The negative values indicate a decrease in stability.