Spurious conformational transitions in proteins?
- 1 June 1981
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 78 (6) , 3551-3553
- https://doi.org/10.1073/pnas.78.6.3551
Abstract
Temperature-dependent dynamic processes in biological macromolecules can produce sharp and reversible transitions in spectroscopic properties that might be misinterpreted as evidence for thermally induced conformational changes. This provides a rational explanation for the paradoxical case of D-amino acid oxidase [EC 1.4.3.3], for which a sharp fluorescence transition at 14.degree. C, not observed by sensitive calorimetry, could be due to a dynamic quenching process of large activation energy, rather than a change in conformational state of the protein. Similar interpretations may be valid in other systems studied by experimental techniques that depend, directly or indirectly, on molecular relaxation processes.This publication has 12 references indexed in Scilit:
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