| Autor: |
Chen H; School of Applied and Engineering Physics, 212 Clark Hall, Cornell University, Ithaca, New York 14853, USA., Ahsan SS, Santiago-Berrios MB, Abruña HD, Webb WW |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of the American Chemical Society [J Am Chem Soc] 2010 Jun 02; Vol. 132 (21), pp. 7244-5. |
| DOI: |
10.1021/ja100500k |
| Abstrakt: |
Quenching of fluorophores by the same proteins that they covalently label is a phenomenon that is neither well-known nor well-characterized. It is often assumed that fluorophores are unperturbed by their target proteins. However, it has been observed that attached fluorophores can be quenched by contact with amino acids within the same protein, and this property has been exploited to report on changing conformational states or intramolecular dynamics of proteins. We show in this communication that fluorescence of Alexa dyes is, in fact, quenched by interactions with Trp, Tyr, Met, and His residues through a combination of static and dynamic quenching mechanisms. In light of this finding, the potential effect of intramolecular quenching should be considered in the interpretation of data that involves quantitative measurements of fluorescence intensity in proteins. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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