We constructed a standardized protein folding kinetics database (PFDB) in which the logarithmic rate constants of all listed proteins are calculated at the standard temperature (25°C). A temperature correction based on the Eyring–Kramers equation was introduced for proteins whose folding kinetics were originally measured at temperatures other than 25°C. We verified the temperature correction by comparing the logarithmic rate constants predicted and experimentally observed at 25°C for 14 different proteins, and the results demonstrated improvement of the quality of the database. PFDB consists of 141 (89 two-state and 52 non-two-state) single-domain globular proteins, which has the largest number among the currently available databases of protein folding kinetics. PFDB is thus intended to be used as a standard for developing and testing future predictive and theoretical studies of protein folding.
The composition of the PFDB in terms of structural and folding class is shown below:
We welcome submissions of protein kinetics folding and unfolding results for addition to the database. Submissions must be associated with an article published in a peer-reviewed publication. To submit an entry, please contact email@example.com