Probing the role of water in protein conformation and function
| Autor: | Rand, R., Ho, M., Littlechild, J., Finney, J., Engberts, J., CUPANE, Antonio |
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| Přispěvatelé: | Rand, R., Ho, M., Littlechild, J., Finney, J., Cupane, A., Engberts, J. |
| Rok vydání: | 2004 |
| Předmět: |
Conformational change
Osmotic shock Protein Conformation Chemical reaction General Biochemistry Genetics and Molecular Biology chemistry.chemical_compound Protein structure Hexokinase Molecular assembly Water hydration Osmotic stre Chemistry Protein Proteins Water Water-Electrolyte Balance Agricultural and Biological Sciences (miscellaneous) Small molecule Settore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin) Glucose Agricultural and Biological Sciences (all) Solubility Biochemistry Intramolecular force Biophysics General Agricultural and Biological Sciences Research Article Macromolecule |
| Zdroj: | Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences. 359:1277-1285 |
| ISSN: | 1471-2970 0962-8436 |
| DOI: | 10.1098/rstb.2004.1504 |
| Popis: | Life began in a bath of water and has never escaped it. Cellular function has forced the evolution of many mechanisms ensuring that cellular water concentration has never changed significantly. To free oneself of any conceptual distinction among all small molecules, solutes and solvents, means that experiments to probe water's specific role in molecular function can be designed like any classical chemical reaction. Such an ‘osmotic stress’ strategy will be described in general and for an enzyme, hexokinase. Water behaves like a reactant that competes with glucose in binding to hexokinase, and modulates its conformational change and activity. This ‘osmotic stress’ strategy, now applied to many very different systems, shows that water plays a significant role, energetically, in most macromolecular reactions. It can be required to fill obligatory space, it dominates nearest non–specific interactions between large surfaces, it can be a reactant modulating conformational change; all this in addition to its more commonly perceived static role as an integral part of stereospecific intramolecular structure. |
| Databáze: | OpenAIRE |
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