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. Author manuscript; available in PMC: 2018 Feb 1.
Published in final edited form as: Curr Opin Struct Biol. 2016 Dec 27;42:98–105. doi: 10.1016/j.sbi.2016.12.002

Table 1.

Rates of spontaneous unfolding and refolding of various protein domains. The first seven protein domains are taken from Table 1 of Jackson [19], which has original references to kinetics data. Data for the FNIII domains are from Shah et al **[20]. The C following the domain number indicates a Cys mutation introduced to measure kinetics by thiol exchange.

Protein Structure PDB ku s−1 kf s−1
Arc repressor α/β 1ARR 1.5 10,600
Monomeric λ repressor (λ6–85) α 1LMB 30 4,900
Villin 14T (headpiece) α/β 1VIK 0.061 900
CspA (B. subtilis) ß-barrel 1MEF 4.2 200
SH3 domain (PI3 kinase) ß 1PKS 0.001 94
Chymotrypsin inhib 2 α/β 1COA 0.00018 48
SH3 domain ß 1AEY 0.045 8.1
FN III-2C ß 2HA1 0.00027 4.8
FN III-3C ß 2N1K 0.0019 0.55
FN III-6C ß 0.000013 0.14
FN III-7 ß 1FNF 0.00007 1.4
FN III-9C ß 1FNF 0.00003 -
FN III-11C ß 0.016 0.06
FN III-12C ß 1FNH 0.00023 0.3
Irisin ß 4LSD 0.0021 1.9
TNfn3C ß 1TEN 0.006 0.72