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Título

Hydrogen-exchange stability analysis of Bergerac-Src homology 3 variants allows the characterization of a folding intermediate in equilibrium

AutorViguera, Ana Rosa; Serrano, Luis
Palabras claveKinetics
β-hairpin
Fecha de publicaciónmay-2003
EditorNational Academy of Sciences (U.S.)
CitaciónProceedings of the National Academy of Sciences 100(10): 5730–5735 (2003)
ResumenAmide 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.
DescripciónCopyright © by National Academy of Sciences. Final full-text version of the paper available at: http://www.pnas.org/content/vol100/issue10/
URIhttp://hdl.handle.net/10261/3558
DOI10.1073/pnas.0837456100
ISSN1091-6490
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