2024-03-28T15:35:01Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/35582021-12-28T15:50:58Zcom_10261_42com_10261_1col_10261_295
Viguera, Ana Rosa
Serrano, Luis
2008-04-14T09:27:49Z
2008-04-14T09:27:49Z
2003-05
Proceedings of the National Academy of Sciences 100(10): 5730–5735 (2003)
1091-6490
http://hdl.handle.net/10261/3558
10.1073/pnas.0837456100
12719536
Amide hydrogen/deuterium exchange rates have been determined for two mutants of α-spectrin Src homology 3 domain (WT), containing an elongated stable (SHH) and unstable (SHA) distal loop. SHA, similarly to WT, follows a two-state transition, whereas SHH apparently folds via a three-state mechanism. Native-state amide hydrogen exchange is effective in ascribing energetic readjustments observed in kinetic experiments to species stabilized within the denatured base and distinguishing those from high-energy barrier crossings. Comparison of ΔGex and mex parameters for amide protons of these mutants demonstrates the existence of an intermediate and allows the identification of protons protected in this state. The consolidation of a form containing a prefolded long β-hairpin induces the switch to a three-state mechanism in an otherwise two-state folder. It can be inferred that the unbalanced high stability of individual elements of secondary structure in a polypeptide could ultimately complicate its folding mechanism.
eng
closedAccess
Kinetics
β-hairpin
Hydrogen-exchange stability analysis of Bergerac-Src homology 3 variants allows the characterization of a folding intermediate in equilibrium
artículo