Tyrosine fluorescence probing of the surfactant-induced conformational changes of albumin
Author:
Affiliation:
1. Department of Physics
2. M.V. Lomonosov Moscow State University
3. Moscow 119991
4. Russia
5. Department of Biology
Abstract
Tyrosine fluorescence in native proteins is known to be effectively quenched, whereas its emission increases upon proteins’ unfolding.
Publisher
Springer Science and Business Media LLC
Subject
Physical and Theoretical Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2015/PP/C4PP00432A
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