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

doi:10.1529/biophysj.108.142448

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

Chemistry

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	169-179
Number of pages	11
Journal	Biophysical journal
Volume	96
Issue number	1
DOIs	https://doi.org/10.1529/biophysj.108.142448
State	Published - Jan 7 2009

ASJC Scopus subject areas

Biophysics

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10.1529/biophysj.108.142448

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title = "Equilibrium unfolding thermodynamics of β2-microglobulin analyzed through native-state H/D exchange",

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.",

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

note = "Funding Information: This work was supported by the Italian Ministero dell'Istruzione, dell'Universit{\`a} e della Ricerca (PRIN 2006_058958, FIRB RBNE03PX83, RBLA03B3KC_0059, and RBNE03B8KK), the Fondazione Cariplo (Progetto Nobel), and the European Union (Sixth Framework Program grant EURAMY). ",

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doi = "10.1529/biophysj.108.142448",

language = "English (US)",

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T1 - Equilibrium unfolding thermodynamics of β2-microglobulin analyzed through native-state H/D exchange

AU - Rennella, Enrico

AU - Corazza, Alessandra

AU - Fogolari, Federico

AU - Viglino, Paolo

AU - Giorgetti, Sofia

AU - Stoppini, Monica

AU - Bellotti, Vittorio

AU - Esposito, Gennaro

N1 - Funding Information: This work was supported by the Italian Ministero dell'Istruzione, dell'Università e della Ricerca (PRIN 2006_058958, FIRB RBNE03PX83, RBLA03B3KC_0059, and RBNE03B8KK), the Fondazione Cariplo (Progetto Nobel), and the European Union (Sixth Framework Program grant EURAMY).

PY - 2009/1/7

Y1 - 2009/1/7

N2 - 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.

AB - 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.

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JO - Biophysical journal

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

Abstract

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