Maltose binding protein (MBP) exhibits a slow phase of folding at pH 7.4, 298 K. The kinetics of this phase has been characterized as a function of denaturant concentration and temperature. Denaturant double-jump experiments and the activation energy for folding indicate that the slow phase involves processes other than proline isomerization. Although the first five N-terminal residues are disordered in the MBP crystal structure, mutations in this region slow down folding and destabilize the native structure. This is the first report showing that disordered N-terminal residues can affect folding kinetics and stability. Copyright (C) 1999 Federation of European Biochemical Societies.
Ganesh, C., Banerjee, A., Shah, A., & Varadarajan, R. (1999). Disordered N-terminal residues affect the folding thermodynamics and kinetics of maltose binding protein. FEBS Letters, 454(3), 307–311. https://doi.org/10.1016/S0014-5793(99)00826-1