Publication: Identifying Sequence Effects on Chain Dimensions of Disordered Proteins by Integrating Experiments and Simulations
Identifying Sequence Effects on Chain Dimensions of Disordered Proteins by Integrating Experiments and Simulations
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Holla, A., Martin, E. W., Dannenhoffer-Lafage, T., Ruff, K. M., König, S. L. B., Nüesch, M. F., Chowdhury, A., Louis, J. M., Soranno, A., Nettels, D., Pappu, R. V., Best, R. B., Mittag, T., & Schuler, B. (2024). Identifying Sequence Effects on Chain Dimensions of Disordered Proteins by Integrating Experiments and Simulations. JACS Au, 4(12), 4729–4743. https://doi.org/10.1021/jacsau.4c00673
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Abstract
It has become increasingly evident that the conformational distributions of intrinsically disordered proteins or regions are strongly dependent on their amino acid compositions and sequence. To facilitate a systematic investigation of these sequence-ensemble relationships, we selected a set of 16 naturally occurring intrinsically disordered regions of identical length but with large differences in amino acid composition, hydrophobicity, and charge patterning. We probed their conformational ensembles with single-molecule Förster resona
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- Holla, Andrea
- Martin, Erik W
- Dannenhoffer-Lafage, Thomas
- Ruff, Kiersten M
- König, Sebastian L B
- Nüesch, Mark F
- Chowdhury, Aritra
- Louis, John M
- Soranno, Andrea
- Nettels, Daniel
- Pappu, Rohit V
- Best, Robert B
- Mittag, Tanja
- Schuler, Benjamin
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Holla, A., Martin, E. W., Dannenhoffer-Lafage, T., Ruff, K. M., König, S. L. B., Nüesch, M. F., Chowdhury, A., Louis, J. M., Soranno, A., Nettels, D., Pappu, R. V., Best, R. B., Mittag, T., & Schuler, B. (2024). Identifying Sequence Effects on Chain Dimensions of Disordered Proteins by Integrating Experiments and Simulations. JACS Au, 4(12), 4729–4743. https://doi.org/10.1021/jacsau.4c00673
