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In-depth interrogation of protein thermal unfolding data with MoltenProt

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In-depth interrogation of protein thermal unfolding data with MoltenProt. / Kotov, Vadim; Mlynek, Georg; Vesper, Oliver; Pletzer, Marina; Wald, Jiri; Teixeira-Duarte, Celso M; Celia, Herve; Garcia-Alai, Maria; Nussberger, Stephan; Buchanan, Susan K; Morais-Cabral, João H; Loew, Christian; Djinovic-Carugo, Kristina; Marlovits, Thomas C.

In: PROTEIN SCI, Vol. 30, No. 1, 01.2021, p. 201-217.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Kotov, V, Mlynek, G, Vesper, O, Pletzer, M, Wald, J, Teixeira-Duarte, CM, Celia, H, Garcia-Alai, M, Nussberger, S, Buchanan, SK, Morais-Cabral, JH, Loew, C, Djinovic-Carugo, K & Marlovits, TC 2021, 'In-depth interrogation of protein thermal unfolding data with MoltenProt', PROTEIN SCI, vol. 30, no. 1, pp. 201-217. https://doi.org/10.1002/pro.3986

APA

Kotov, V., Mlynek, G., Vesper, O., Pletzer, M., Wald, J., Teixeira-Duarte, C. M., Celia, H., Garcia-Alai, M., Nussberger, S., Buchanan, S. K., Morais-Cabral, J. H., Loew, C., Djinovic-Carugo, K., & Marlovits, T. C. (2021). In-depth interrogation of protein thermal unfolding data with MoltenProt. PROTEIN SCI, 30(1), 201-217. https://doi.org/10.1002/pro.3986

Vancouver

Kotov V, Mlynek G, Vesper O, Pletzer M, Wald J, Teixeira-Duarte CM et al. In-depth interrogation of protein thermal unfolding data with MoltenProt. PROTEIN SCI. 2021 Jan;30(1):201-217. https://doi.org/10.1002/pro.3986

Bibtex

@article{2e2e3f2020d846c1b47142cb822d2774,
title = "In-depth interrogation of protein thermal unfolding data with MoltenProt",
abstract = "Protein stability is a key factor in successful structural and biochemical research. However, the approaches for systematic comparison of protein stability are limited by sample consumption or compatibility with sample buffer components. Here we describe how miniaturized measurement of intrinsic tryptophan fluorescence (NanoDSF assay) in combination with a simplified description of protein unfolding can be used to interrogate the stability of a protein sample. We demonstrate that improved protein stability measures, such as apparent Gibbs free energy of unfolding, rather than melting temperature Tm , should be used to rank the results of thermostability screens. The assay is compatible with protein samples of any composition, including protein complexes and membrane proteins. Our data analysis software, MoltenProt, provides an easy and robust way to perform characterization of multiple samples. Potential applications of MoltenProt and NanoDSF include buffer and construct optimization for X-ray crystallography and cryo-electron microscopy, screening for small-molecule binding partners and comparison of effects of point mutations.",
author = "Vadim Kotov and Georg Mlynek and Oliver Vesper and Marina Pletzer and Jiri Wald and Teixeira-Duarte, {Celso M} and Herve Celia and Maria Garcia-Alai and Stephan Nussberger and Buchanan, {Susan K} and Morais-Cabral, {Jo{\~a}o H} and Christian Loew and Kristina Djinovic-Carugo and Marlovits, {Thomas C}",
note = "{\textcopyright} 2020 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.",
year = "2021",
month = jan,
doi = "10.1002/pro.3986",
language = "English",
volume = "30",
pages = "201--217",
journal = "PROTEIN SCI",
issn = "0961-8368",
publisher = "Cold Spring Harbor Laboratory Press",
number = "1",

}

RIS

TY - JOUR

T1 - In-depth interrogation of protein thermal unfolding data with MoltenProt

AU - Kotov, Vadim

AU - Mlynek, Georg

AU - Vesper, Oliver

AU - Pletzer, Marina

AU - Wald, Jiri

AU - Teixeira-Duarte, Celso M

AU - Celia, Herve

AU - Garcia-Alai, Maria

AU - Nussberger, Stephan

AU - Buchanan, Susan K

AU - Morais-Cabral, João H

AU - Loew, Christian

AU - Djinovic-Carugo, Kristina

AU - Marlovits, Thomas C

N1 - © 2020 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.

PY - 2021/1

Y1 - 2021/1

N2 - Protein stability is a key factor in successful structural and biochemical research. However, the approaches for systematic comparison of protein stability are limited by sample consumption or compatibility with sample buffer components. Here we describe how miniaturized measurement of intrinsic tryptophan fluorescence (NanoDSF assay) in combination with a simplified description of protein unfolding can be used to interrogate the stability of a protein sample. We demonstrate that improved protein stability measures, such as apparent Gibbs free energy of unfolding, rather than melting temperature Tm , should be used to rank the results of thermostability screens. The assay is compatible with protein samples of any composition, including protein complexes and membrane proteins. Our data analysis software, MoltenProt, provides an easy and robust way to perform characterization of multiple samples. Potential applications of MoltenProt and NanoDSF include buffer and construct optimization for X-ray crystallography and cryo-electron microscopy, screening for small-molecule binding partners and comparison of effects of point mutations.

AB - Protein stability is a key factor in successful structural and biochemical research. However, the approaches for systematic comparison of protein stability are limited by sample consumption or compatibility with sample buffer components. Here we describe how miniaturized measurement of intrinsic tryptophan fluorescence (NanoDSF assay) in combination with a simplified description of protein unfolding can be used to interrogate the stability of a protein sample. We demonstrate that improved protein stability measures, such as apparent Gibbs free energy of unfolding, rather than melting temperature Tm , should be used to rank the results of thermostability screens. The assay is compatible with protein samples of any composition, including protein complexes and membrane proteins. Our data analysis software, MoltenProt, provides an easy and robust way to perform characterization of multiple samples. Potential applications of MoltenProt and NanoDSF include buffer and construct optimization for X-ray crystallography and cryo-electron microscopy, screening for small-molecule binding partners and comparison of effects of point mutations.

U2 - 10.1002/pro.3986

DO - 10.1002/pro.3986

M3 - SCORING: Journal article

C2 - 33140490

VL - 30

SP - 201

EP - 217

JO - PROTEIN SCI

JF - PROTEIN SCI

SN - 0961-8368

IS - 1

ER -