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Title: “Turn-On” Protein Fluorescence: In Situ Formation of Cyanine Dyes

Abstract

Protein reengineering of cellular retinoic acid binding protein II (CRABPII) has yielded a genetically addressable system, capable of binding a profluorophoric chromophore that results in fluorescent protein/chromophore complexes. These complexes exhibit far-red emission, with high quantum efficiencies and brightness and also exhibit excellent pH stability spanning the range of 2$-$11. In the course of this study, it became evident that single mutations of L121E and R59W were most effective in improving the fluorescent characteristics of CRABPII mutants as well as the kinetics of complex formation. The readily crystallizable nature of these proteins was invaluable to provide clues for the observed spectroscopic behavior that results from single mutation of key residues.

Authors:
 [1];  [1];  [1];  [1];  [1];  [1];  [1];  [1];  [1];  [1]
  1. Michigan State Univ., East Lansing, MI (United States). Dept. of Chemistry
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1237768
Grant/Contract Number:  
W-31-109-ENG-38
Resource Type:
Accepted Manuscript
Journal Name:
Journal of the American Chemical Society
Additional Journal Information:
Journal Volume: 137; Journal Issue: 3; Journal ID: ISSN 0002-7863
Publisher:
American Chemical Society (ACS)
Country of Publication:
United States
Language:
ENGLISH
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY

Citation Formats

Yapici, Ipek, Lee, Kin Sing Stephen, Berbasova, Tetyana, Nosrati, Meisam, Jia, Xiaofei, Vasileiou, Chrysoula, Wang, Wenjing, Santos, Elizabeth M., Geiger, James H., and Borhan, Babak. “Turn-On” Protein Fluorescence: In Situ Formation of Cyanine Dyes. United States: N. p., 2014. Web. doi:10.1021/ja506376j.
Yapici, Ipek, Lee, Kin Sing Stephen, Berbasova, Tetyana, Nosrati, Meisam, Jia, Xiaofei, Vasileiou, Chrysoula, Wang, Wenjing, Santos, Elizabeth M., Geiger, James H., & Borhan, Babak. “Turn-On” Protein Fluorescence: In Situ Formation of Cyanine Dyes. United States. doi:10.1021/ja506376j.
Yapici, Ipek, Lee, Kin Sing Stephen, Berbasova, Tetyana, Nosrati, Meisam, Jia, Xiaofei, Vasileiou, Chrysoula, Wang, Wenjing, Santos, Elizabeth M., Geiger, James H., and Borhan, Babak. Mon . "“Turn-On” Protein Fluorescence: In Situ Formation of Cyanine Dyes". United States. doi:10.1021/ja506376j. https://www.osti.gov/servlets/purl/1237768.
@article{osti_1237768,
title = {“Turn-On” Protein Fluorescence: In Situ Formation of Cyanine Dyes},
author = {Yapici, Ipek and Lee, Kin Sing Stephen and Berbasova, Tetyana and Nosrati, Meisam and Jia, Xiaofei and Vasileiou, Chrysoula and Wang, Wenjing and Santos, Elizabeth M. and Geiger, James H. and Borhan, Babak},
abstractNote = {Protein reengineering of cellular retinoic acid binding protein II (CRABPII) has yielded a genetically addressable system, capable of binding a profluorophoric chromophore that results in fluorescent protein/chromophore complexes. These complexes exhibit far-red emission, with high quantum efficiencies and brightness and also exhibit excellent pH stability spanning the range of 2$-$11. In the course of this study, it became evident that single mutations of L121E and R59W were most effective in improving the fluorescent characteristics of CRABPII mutants as well as the kinetics of complex formation. The readily crystallizable nature of these proteins was invaluable to provide clues for the observed spectroscopic behavior that results from single mutation of key residues.},
doi = {10.1021/ja506376j},
journal = {Journal of the American Chemical Society},
number = 3,
volume = 137,
place = {United States},
year = {2014},
month = {12}
}

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