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. Author manuscript; available in PMC: 2010 Jun 17.
Published in final edited form as: J Am Chem Soc. 2007 Oct 2;129(42):12801–12808. doi: 10.1021/ja073366l

Table 1.

Survey of helix-coil studies that included the temperature dependence of T-jump relaxations.

Peptide Monitor Ti, °C T, °C Apparent Ea (kcal mol−1)⊥ Ref.
Ac-WA3H+-(AAAR+A)3A Fluorescence varied ~10.0 8.0 [3]
A5(A3RA)3A UVRR 4.0 varied * [10]
YGG(KA4)3COR IR varied ~10.0 15.5 [4]
AcYGSPEA3KA4KA4-DArg-CONH2 (Ac-Y-GSP peptide) IR varied ~10.0 11.5 [8]
[Rub2m]2+-CONH-AAAAA(AAARA)3A-CONH2 IR varied ~10.0 13.5 [19]
Ac-GSP peptide UVRR 6.0 varied 0.1 Current Work
GSP peptide varied 10 5.4 Current Work
⊥

Obtained from the Arrhenius plots of the relaxation rate following the T-jumps.

*

A factor of 3 acceleration between Tf = 33 and 65° was decomposed via the helix/coil equilibrium constant into apparent Ea’s of 8.0 and −4.0 for unfolding and folding rates, assuming a 2-state kinetic model.