The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Protein stability and enzyme activity at extreme biological temperatures
Open accessAbstract
Psychrophilic microorganisms thrive in permanently cold environments, even at subzero temperatures. To maintain metabolic rates compatible with sustained life, they have improved the dynamics of their protein structures, thereby enabling appropriate molecular motions required for biological activity at low temperatures. As a consequence of this structural flexibility, psychrophilic proteins are unstable and heat-labile. In the upper range of biological temperatures, thermophiles and hyperthermophiles grow at temperatures > 100 °C and synthesize ultra-stable proteins. However, thermophilic enzymes are nearly inactive at room temperature as a result of their compactness and rigidity. At the molecular level, both types of extremophilic proteins have adapted the same structural factors, but in opposite directions, to address either activity at low temperatures or stability in hot environments. A model based on folding funnels is proposed accounting for the stability-activity relationships in extremophilic proteins.
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Takai, K., Nakamura, K., Toki, T., Tsunogai, U., Miyazaki, M., Miyazaki, J., Hirayama, H., Nakagawa, S., Nunoura, T., & Horikoshi, K. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712334105 · Cited by 848
Folding funnels, binding funnels, and protein function
Tsai, C., Kumar, S., Ma, B., & Nussinov, R. (1999) · Protein Science · doi:10.1110/ps.8.6.1181 · Cited by 648
On the rocks: the microbiology of Antarctic Dry Valley soils
Cary, S. C., McDonald, I. R., Barrett, J. E., & Cowan, D. A. (2010) · Nature Reviews Microbiology · doi:10.1038/nrmicro2281 · Cited by 580
Ancient bacteria show evidence of DNA repair
Johnson, S. S., Hebsgaard, M. B., Christensen, T. R., Mastepanov, M., Nielsen, R., Munch, K., Brand, T., Gilbert, M. T. P., Zuber, M. T., Bunce, M., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706787104 · Cited by 292
Transition-state Ensemble in Enzyme Catalysis: Possibility, Reality, or Necessity?
MA, B., KUMAR, S., TSAI, C.-J., HU, Z., & NUSSINOV, R. (2000) · Journal of Theoretical Biology · doi:10.1006/jtbi.2000.1097 · Cited by 86
Cited by
Cui, S., Dasgupta, S., Yagi, S., Kimura, M., Furukawa, R., Tagami, S., & Akanuma, S. (2025) · Protein Science · doi:10.1002/pro.70071 · Cited by 12
Seal, S., Baruah, M., Majgaonkar, A., Altaf, M., De, P., Umair, M., Sohail, M., & Sinha, D. (2024) · Trends in Biotechnology of Polyextremophiles · doi:10.1007/978-3-031-55032-4_19 · Cited by 3
Introduction of multiple disulfide bonds increases the thermostability of transglutaminase
Ono, T., Takahashi, K., Hirao, Y., Mihara, Y., Abe, I., Shirasawa, A., & Sugiki, M. (2025) · Scientific Reports · doi:10.1038/s41598-025-07842-5 · Cited by 2
Metadata
- Authors
- Feller, G.
- Venue
- Journal of Physics: Condensed Matter
- Publisher
- IOP Publishing
- Published
- 2010-07-07
- Volume
- 22
- Issue
- 32
- Pages
- 323101
- ISSN
- 0953-8984 (ISSN-L)
- 1361-648X
- OpenAlex
- W1992888813
- Cited by
- 337
- References
- 5
- FWCI
- 6.62
- Type
- journal article
- Language
- en
- Open access
- green
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