Maleimido-proxyl as an EPR spin label for the evaluation of conformational changes of albumin-Reference-Cited by-同舟云学术

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Maleimido-proxyl as an EPR spin label for the evaluation of conformational changes of albumin

Published:2017-09-23 Issue:8 Volume:46 Page:773-787
ISSN:0175-7571
Container-title:European Biophysics Journal
language:en
Short-container-title:Eur Biophys J

Author:

Pavićević Aleksandra,Luo Jinghui,Popović-Bijelić Ana,Mojović Miloš

Funder

Ministry of Education, Science and Technological Development of the Republic of Serbia

Publisher

Springer Science and Business Media LLC

Subject

General Medicine,Biophysics

Link

http://link.springer.com/article/10.1007/s00249-017-1257-z/fulltext.html

Reference93 articles.

1. Akdogan Y, Hinderberger D (2011) Solvent-induced protein refolding at low temperatures. J Phys Chem B 115:15422–15429. doi: 10.1021/jp209646f

2. Akdogan Y, Junk MJN, Hinderberger D (2011) Effect of ionic liquids on the solution structure of human serum albumin. Biomacromol 12:1072–1079. doi: 10.1021/bm1014156

3. Akdogan Y, Reichenwallner J, Hinderberger D (2012a) Evidence for water-tuned structural differences in proteins: an approach emphasizing variations in local hydrophilicity. PLoS One 7:e45681. doi: 10.1371/journal.pone.0045681

4. Akdogan Y, Wu Y, Eisele K et al (2012b) Host–guest interactions in polycationic human serum albumin bioconjugates. Soft Matter 8:11106–11114. doi: 10.1039/C2SM26511G

5. Anjos JLV, Santiago PS, Tabak M, Alonso A (2011) On the interaction of bovine serum albumin with ionic surfactants: temperature induced EPR changes of a maleimide nitroxide reflect local protein dynamics and probe solvent accessibility. Colloids Surf B 88:463–470. doi: 10.1016/j.colsurfb.2011.07.030

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