Thermal denaturation and folding rates of single domain proteins: size matters
| dc.creator | Li, Mai Suan | |
| dc.creator | Klimov, D. K. | |
| dc.creator | Thirumalai, D. | |
| dc.date | 2003-10-16 | |
| dc.date.accessioned | 2026-07-07T05:57:55Z | |
| dc.date.available | 2026-07-07T05:57:55Z | |
| dc.description | We analyze the dependence of thermal denaturation transition and folding rates of globular proteins on the number of amino acid residues, N. Using lattice Go models we show that DeltaT/T_F ~ N^-1, where T_F is the folding transition temperature and DeltaT is the folding transition width. This finding is consistent with finite size effects expected for the systems undergoing a phase transition from a disordered to an ordered phase. The dependence of the folding rates k_F on N for lattice models and the dataset of 57 proteins and peptides shows that k_F = k_F^0 exp(-CN^beta) provides a good fit, if 0 < beta <= 2/3 and C is a constant. We find that k_F = k_F^0 exp(-1.1N^0.5) with k_F^0 =(0.4x10^-6 s)^-1 can estimate optimal protein folding rates to within an order of magnitude in most cases. By using this fit for a set of proteins with beta-sheet topology we find that k_F^0 is approximately equal to k_U^0, the prefactor for unfolding rates. The maximum ratio of k_U^0/k_F^0 is 10 for this class of proteins. | |
| dc.description | 11 pages, 3 figures | |
| dc.identifier | https://arxiv.org/abs/q-bio/0310020 | |
| dc.identifier | http://arxiv.org/abs/q-bio/0310020 | |
| dc.identifier.uri | http://salesiana.dossiersoluciones.com/handle/123456789/88167 | |
| dc.subject | Biomolecules | |
| dc.title | Thermal denaturation and folding rates of single domain proteins: size matters | |
| dc.type | text |