Equilibrium unfolding thermodynamics of β2-microglobulin analyzed through native-state H/D exchange

Enrico Rennella, Alessandra Corazza, Federico Fogolari, Paolo Viglino, Sofia Giorgetti, Monica Stoppini, Vittorio Bellotti, Gennaro Esposito

    Research output: Contribution to journalArticle

    Abstract

    The exchange rates for the amide hydrogens of β2- microglobulin, the protein responsible for dialysis-related amyloidosis, were measured under native conditions at different temperatures ranging from 301 to 315 K. The pattern of protection factors within different regions of the protein correlates well with the hydrogen-bonding pattern of the deposited structures. Analysis of the exchange rates indicates the presence of mixed EX1- and EX2-limit mechanisms. The measured parameters are consistent with a two-process model in which two competing pathways, i.e., global unfolding in the core region and partial openings of the native state, determine the observed exchange rates. These findings are analyzed with respect to the amyloidogenic properties of the protein.

    Original languageEnglish (US)
    Pages (from-to)169-179
    Number of pages11
    JournalBiophysical Journal
    Volume96
    Issue number1
    DOIs
    StatePublished - Jan 7 2009

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    Thermodynamics
    Amyloidogenic Proteins
    Amyloidosis
    Hydrogen Bonding
    Amides
    Dialysis
    Hydrogen
    Proteins
    Temperature

    ASJC Scopus subject areas

    • Biophysics

    Cite this

    Rennella, E., Corazza, A., Fogolari, F., Viglino, P., Giorgetti, S., Stoppini, M., ... Esposito, G. (2009). Equilibrium unfolding thermodynamics of β2-microglobulin analyzed through native-state H/D exchange. Biophysical Journal, 96(1), 169-179. https://doi.org/10.1529/biophysj.108.142448

    Equilibrium unfolding thermodynamics of β2-microglobulin analyzed through native-state H/D exchange. / Rennella, Enrico; Corazza, Alessandra; Fogolari, Federico; Viglino, Paolo; Giorgetti, Sofia; Stoppini, Monica; Bellotti, Vittorio; Esposito, Gennaro.

    In: Biophysical Journal, Vol. 96, No. 1, 07.01.2009, p. 169-179.

    Research output: Contribution to journalArticle

    Rennella, E, Corazza, A, Fogolari, F, Viglino, P, Giorgetti, S, Stoppini, M, Bellotti, V & Esposito, G 2009, 'Equilibrium unfolding thermodynamics of β2-microglobulin analyzed through native-state H/D exchange', Biophysical Journal, vol. 96, no. 1, pp. 169-179. https://doi.org/10.1529/biophysj.108.142448
    Rennella, Enrico ; Corazza, Alessandra ; Fogolari, Federico ; Viglino, Paolo ; Giorgetti, Sofia ; Stoppini, Monica ; Bellotti, Vittorio ; Esposito, Gennaro. / Equilibrium unfolding thermodynamics of β2-microglobulin analyzed through native-state H/D exchange. In: Biophysical Journal. 2009 ; Vol. 96, No. 1. pp. 169-179.
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    AU - Giorgetti, Sofia

    AU - Stoppini, Monica

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