Spurious conformational transitions in proteins?
AUTOR(ES)
Cooper, A
RESUMO
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 [D-amino-acid:oxygen oxidoreductase (deaminating), EC 1.4.3.3], for which a sharp fluorescence transition at 14 degrees C, not observed by sensitive calorimetry [Sturtevant, J. M. & Mateo, P. L. (1978) Proc. Natl. Acad. Sci. USA 75, 2584-2587], 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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=319607Documentos Relacionados
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