Kinetic and thermodynamic parameters for the folding of dimeric proteins

Range Table - link
Organism Unspecified
Reference Jackson SE. How do small single-domain proteins fold? Fold Des. 1998 3(4):R81-91. DOI: 10.1016/S1359-0278(98)00033-9 p.R88 table 3PubMed ID9710577
Primary Source See refs beneath table
Comments P.R88 right column 3rd paragraph: "Comparison of the folding of monomeric and dimeric proteins: Thermodynamic and kinetic data for the folding of three dimeric proteins are summarised in Table 3. The folding of the Arc represssor [primary sources 78–81] and GCN-4 [primary source 82] is concurrent with dimerisation, whereas the rate-determining step in the folding of the ROP dimer is unimolecular [primary source 51]. Thus, there is a rate-limiting structural rearrangement after the fast association of two chains. Dimeric proteins, like small monomeric proteins, can fold with simple two-state kinetics or via populated intermediate states. The range of folding rates (at 10 μM protein) and βT are within the range found for monomeric proteins. Thus, it appears that there are no intrinsic differences between the folding of monomers and dimers." See notes beneath table
Entered by Uri M
ID 114416