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. 2005 Jun;14(6):1643–1660. doi: 10.1110/ps.041317705

Table 1.

Data for the four proteins studied

Protein Pdb N Rng (Å) kf (sec−1) Texp (°C)
Acylphosphatase 1aps 98 12.6 2.3 × 10−1 28
Chymotrypsin inhibitor 2 2ci2 64 10.8 4.8 × 101 25
Spliceosomal protein U1A 1urn 96 12.2 3.2 × 102 25
λ-repressor 1lmb 80 11.5 1.1 × 104 25

Protein databank id, pdb; number of amino acids, N; radius of gyration, Rng; and experimental folding rate in water, kf, determined at temperature Texp (Jackson and Fersht 1991; Silow and Oliveberg 1997; van Nuland et al. 1998; Myers and Oas 1999).