The DOI matches its Crossref record; 74 of the 74 references it cites were found in a registry or an index.
Rigidity versus flexibility: the dilemma of understanding protein thermal stability
Open accessAbstract
The role of fluctuations in protein thermostability has recently received considerable attention. In the current literature a dualistic picture can be found: thermostability seems to be associated with enhanced rigidity of the protein scaffold in parallel with the reduction of flexible parts of the structure. In contradiction to such arguments it has been shown by experimental studies and computer simulation that thermal tolerance of a protein is not necessarily correlated with the suppression of internal fluctuations and mobility. Both concepts, rigidity and flexibility, are derived from mechanical engineering and represent temporally insensitive features describing static properties, neglecting that relative motion at certain time scales is possible in structurally stable regions of a protein. This suggests that a strict separation of rigid and flexible parts of a protein molecule does not describe the reality correctly. In this work the concepts of mobility/flexibility versus rigidity will be critically reconsidered by taking into account molecular dynamics calculations of heat capacity and conformational entropy, salt bridge networks, electrostatic interactions in folded and unfolded states, and the emerging picture of protein thermostability in view of recently developed network theories. Last, but not least, the influence of high temperature on the active site and activity of enzymes will be considered.
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Cites
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Buß, O., Rudat, J., & Ochsenreither, K. (2018) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2018.01.002 · Cited by 284
Walker, E. J., Bettinger, J. Q., Welle, K. A., Hryhorenko, J. R., Molina Vargas, A. M., O’Connell, M. R., & Ghaemmaghami, S. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101872 · Cited by 35
Amino acid sequence encodes protein abundance shaped by protein stability at reduced synthesis cost
(2024) · doi:10.1002/pro.5239 · Cited by 12
Komp, E., Alanzi, H. N., Francis, R., Vuong, C., Roberts, L., Mosallanejad, A., & Beck, D. A. C. (2023) · Scientific Data · doi:10.1038/s41597-023-02553-w · Cited by 7
Shukla, D., Martin, J., Morcos, F., & Potoyan, D. A. (2025) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.4c01774 · Cited by 4
Metadata
- Authors
- Karshikoff, A., Nilsson, L., & Ladenstein, R.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2015-07-15
- Volume
- 282
- Issue
- 20
- Pages
- 3899-3917
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W1848447147
- Cited by
- 281
- References
- 74
- FWCI
- 8.23
- Type
- journal article
- Language
- en
- Open access
- bronze
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