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PKa values for the unfolded state under native conditions explain the pH-dependent stability of PGB1

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PKa values for the unfolded state under native conditions explain the pH-dependent stability of PGB1. / Lindman, Stina; Bauer, Mikael C.; Lund, Mikael et al.
In: Biophysical Journal, Vol. 99, No. 10, 17.11.2010, p. 3365-3373.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Harvard

Lindman, S, Bauer, MC, Lund, M, Diehl, C, Mulder, FAA, Akke, M & Linse, S 2010, 'PKa values for the unfolded state under native conditions explain the pH-dependent stability of PGB1', Biophysical Journal, vol. 99, no. 10, pp. 3365-3373. https://doi.org/10.1016/j.bpj.2010.08.078

APA

Lindman, S., Bauer, M. C., Lund, M., Diehl, C., Mulder, F. A. A., Akke, M., & Linse, S. (2010). PKa values for the unfolded state under native conditions explain the pH-dependent stability of PGB1. Biophysical Journal, 99(10), 3365-3373. https://doi.org/10.1016/j.bpj.2010.08.078

CBE

Lindman S, Bauer MC, Lund M, Diehl C, Mulder FAA, Akke M, Linse S. 2010. PKa values for the unfolded state under native conditions explain the pH-dependent stability of PGB1. Biophysical Journal. 99(10):3365-3373. https://doi.org/10.1016/j.bpj.2010.08.078

MLA

Lindman, Stina et al. "PKa values for the unfolded state under native conditions explain the pH-dependent stability of PGB1". Biophysical Journal. 2010, 99(10). 3365-3373. https://doi.org/10.1016/j.bpj.2010.08.078

Vancouver

Lindman S, Bauer MC, Lund M, Diehl C, Mulder FAA, Akke M et al. PKa values for the unfolded state under native conditions explain the pH-dependent stability of PGB1. Biophysical Journal. 2010 Nov 17;99(10):3365-3373. doi: 10.1016/j.bpj.2010.08.078

Author

Lindman, Stina ; Bauer, Mikael C. ; Lund, Mikael et al. / PKa values for the unfolded state under native conditions explain the pH-dependent stability of PGB1. In: Biophysical Journal. 2010 ; Vol. 99, No. 10. pp. 3365-3373.

Bibtex

@article{99dad184d568448cbc3ccb730f7a9a52,
title = "PKa values for the unfolded state under native conditions explain the pH-dependent stability of PGB1",
abstract = "Understanding the role of electrostatics in protein stability requires knowledge of these interactions in both the folded and unfolded states. Electrostatic interactions can be probed experimentally by characterizing ionization equilibria of titrating groups, parameterized as pKa values. However, pKa values of the unfolded state are rarely accessible under native conditions, where the unfolded state has a very low population. Here, we report pKa values under nondenaturing conditions for two unfolded fragments of the protein G B1 domain that mimic the unfolded state of the intact protein. pKa values were determined for carboxyl groups by monitoring their pH-dependent 13C chemical shifts. Monte Carlo simulations using a Gaussian chain model provide corrections for changes in electrostatic interactions that arise from fragmentation of the protein. Most pKa values for the unfolded state agree well with model values, but some residues show significant perturbations that can be rationalized by local electrostatic interactions. The pH-dependent stability was calculated from the experimental pKa values of the folded and unfolded states and compared to experimental stability data. The use of experimental pKa values for the unfolded state results in significantly improved agreement with experimental data, as compared to calculations based on model data alone.",
author = "Stina Lindman and Bauer, {Mikael C.} and Mikael Lund and Carl Diehl and Mulder, {Frans A A} and Mikael Akke and Sara Linse",
year = "2010",
month = nov,
day = "17",
doi = "10.1016/j.bpj.2010.08.078",
language = "English",
volume = "99",
pages = "3365--3373",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Cell Press",
number = "10",

}

RIS

TY - JOUR

T1 - PKa values for the unfolded state under native conditions explain the pH-dependent stability of PGB1

AU - Lindman, Stina

AU - Bauer, Mikael C.

AU - Lund, Mikael

AU - Diehl, Carl

AU - Mulder, Frans A A

AU - Akke, Mikael

AU - Linse, Sara

PY - 2010/11/17

Y1 - 2010/11/17

N2 - Understanding the role of electrostatics in protein stability requires knowledge of these interactions in both the folded and unfolded states. Electrostatic interactions can be probed experimentally by characterizing ionization equilibria of titrating groups, parameterized as pKa values. However, pKa values of the unfolded state are rarely accessible under native conditions, where the unfolded state has a very low population. Here, we report pKa values under nondenaturing conditions for two unfolded fragments of the protein G B1 domain that mimic the unfolded state of the intact protein. pKa values were determined for carboxyl groups by monitoring their pH-dependent 13C chemical shifts. Monte Carlo simulations using a Gaussian chain model provide corrections for changes in electrostatic interactions that arise from fragmentation of the protein. Most pKa values for the unfolded state agree well with model values, but some residues show significant perturbations that can be rationalized by local electrostatic interactions. The pH-dependent stability was calculated from the experimental pKa values of the folded and unfolded states and compared to experimental stability data. The use of experimental pKa values for the unfolded state results in significantly improved agreement with experimental data, as compared to calculations based on model data alone.

AB - Understanding the role of electrostatics in protein stability requires knowledge of these interactions in both the folded and unfolded states. Electrostatic interactions can be probed experimentally by characterizing ionization equilibria of titrating groups, parameterized as pKa values. However, pKa values of the unfolded state are rarely accessible under native conditions, where the unfolded state has a very low population. Here, we report pKa values under nondenaturing conditions for two unfolded fragments of the protein G B1 domain that mimic the unfolded state of the intact protein. pKa values were determined for carboxyl groups by monitoring their pH-dependent 13C chemical shifts. Monte Carlo simulations using a Gaussian chain model provide corrections for changes in electrostatic interactions that arise from fragmentation of the protein. Most pKa values for the unfolded state agree well with model values, but some residues show significant perturbations that can be rationalized by local electrostatic interactions. The pH-dependent stability was calculated from the experimental pKa values of the folded and unfolded states and compared to experimental stability data. The use of experimental pKa values for the unfolded state results in significantly improved agreement with experimental data, as compared to calculations based on model data alone.

U2 - 10.1016/j.bpj.2010.08.078

DO - 10.1016/j.bpj.2010.08.078

M3 - Journal article

C2 - 21081085

AN - SCOPUS:78549261090

VL - 99

SP - 3365

EP - 3373

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 10

ER -