Life at low temperatures: is disorder the driving force?
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| Title: | Life at low temperatures: is disorder the driving force? |
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| Authors: | Feller, Georges |
| Source: | Extremophiles. 11:211-216 |
| Publisher Information: | Springer Science and Business Media LLC, 2006. |
| Publication Year: | 2006 |
| Subject Terms: | 0301 basic medicine, Membrane Fluidity, ligand binding, Entropy, Membrane Fluidity/physiology, Bacteria/growth & development/metabolism, Biochimie, biophysique & biologie moléculaire, 03 medical and health sciences, RNA, Transfer/metabolism, Bacterial Proteins, RNA, Transfer, psychrophiles, 0303 health sciences, RNA, Bacterial/metabolism, Bacteria, Bacterial Proteins/metabolism, stability, Life sciences, Adaptation, Physiological, proteins, 3. Good health, Fatty Acids, Unsaturated/metabolism, Cold Temperature, RNA, Bacterial, Sciences du vivant, Fatty Acids, Unsaturated, Biochemistry, biophysics & molecular biology |
| Description: | The thermodynamic characterization of various biological systems from psychrophiles points to a larger entropic contribution when compared to the corresponding mesophilic or (hyper) thermophilic counterparts, either at the level of the macromolecules (thermodynamic and kinetic stabilities) or of their function (ligand binding, catalytic activity). It is suggested here that in an environment characterized by a low heat content (enthalpy) and at temperatures that strongly slowdown molecular motions, the cold-adapted biological systems rely on a larger disorder to maintain macromolecular dynamics and function. Such pre-eminent involvement of entropy is observed in the experimental results and, from a macroscopic point of view, is also reflected for instance by the steric hindrances introduced by cis-unsaturated and branched lipids to maintain membrane fluidity, by the loose conformation of psychrophilic proteins or by the local destabilization of tRNA by dihydrouridine in psychrophilic bacteria. |
| Document Type: | Article |
| Language: | English |
| ISSN: | 1433-4909 1431-0651 |
| DOI: | 10.1007/s00792-006-0050-1 |
| Access URL: | https://pubmed.ncbi.nlm.nih.gov/17160345 http://orbi.ulg.ac.be/handle/2268/14513 https://link.springer.com/content/pdf/10.1007%2Fs00792-006-0050-1.pdf https://link.springer.com/article/10.1007/s00792-006-0050-1 https://orbi.uliege.be/handle/2268/14513 https://hdl.handle.net/2268/14513 https://doi.org/10.1007/s00792-006-0050-1 |
| Rights: | Springer TDM |
| Accession Number: | edsair.doi.dedup.....81ff120b9f75f2baa04b5bf52014517c |
| Database: | OpenAIRE |
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Nájsť tento článok vo Web of Science | Abstract: | The thermodynamic characterization of various biological systems from psychrophiles points to a larger entropic contribution when compared to the corresponding mesophilic or (hyper) thermophilic counterparts, either at the level of the macromolecules (thermodynamic and kinetic stabilities) or of their function (ligand binding, catalytic activity). It is suggested here that in an environment characterized by a low heat content (enthalpy) and at temperatures that strongly slowdown molecular motions, the cold-adapted biological systems rely on a larger disorder to maintain macromolecular dynamics and function. Such pre-eminent involvement of entropy is observed in the experimental results and, from a macroscopic point of view, is also reflected for instance by the steric hindrances introduced by cis-unsaturated and branched lipids to maintain membrane fluidity, by the loose conformation of psychrophilic proteins or by the local destabilization of tRNA by dihydrouridine in psychrophilic bacteria. |
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| ISSN: | 14334909 14310651 |
| DOI: | 10.1007/s00792-006-0050-1 |