Engineering ESPT Pathways Based on Structural Analysis of LSSmKate Red Fluorescent Proteins with Large Stokes Shift-Reference-Cited by-同舟云学术

Engineering ESPT Pathways Based on Structural Analysis of LSSmKate Red Fluorescent Proteins with Large Stokes Shift

Published:2010-07-20 Issue:31 Volume:132 Page:10762-10770
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Piatkevich Kiryl D.¹,Malashkevich Vladimir N.¹,Almo Steven C.¹,Verkhusha Vladislav V.¹

Affiliation:

1. Department of Anatomy and Structural Biology, Gruss-Lipper Biophotonics Center, and Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja101974k

Reference32 articles.

1. Bright far-red fluorescent protein for whole-body imaging

2. Monomeric red fluorescent proteins with a large Stokes shift

3. A fluorescent variant of a protein from the stony coral Montipora facilitates dual-color single-laser fluorescence cross-correlation spectroscopy

4. Reverse pH-Dependence of Chromophore Protonation Explains the Large Stokes Shift of the Red Fluorescent Protein mKeima

5. Excited State Proton Transfer in the Red Fluorescent Protein mKeima

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