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A photoswitchable orange-to-far-red fluorescent protein, PSmOrange.
Nat Methods 2011; 8(9):771-7NM

Abstract

We report a photoswitchable monomeric Orange (PSmOrange) protein that is initially orange (excitation, 548 nm; emission, 565 nm) but becomes far-red (excitation, 636 nm; emission, 662 nm) after irradiation with blue-green light. Compared to its parental orange proteins, PSmOrange has greater brightness, faster maturation, higher photoconversion contrast and better photostability. The red-shifted spectra of both forms of PSmOrange enable its simultaneous use with cyan-to-green photoswitchable proteins to study four intracellular populations. Photoconverted PSmOrange has, to our knowledge, the most far-red excitation peak of all GFP-like fluorescent proteins, provides diffraction-limited and super-resolution imaging in the far-red light range, is optimally excited with common red lasers, and can be photoconverted subcutaneously in a mouse. PSmOrange photoswitching occurs via a two-step photo-oxidation process, which causes cleavage of the polypeptide backbone. The far-red fluorescence of photoconverted PSmOrange results from a new chromophore containing N-acylimine with a co-planar carbon-oxygen double bond.

Authors+Show Affiliations

Department of Anatomy and Structural Biology, and Gruss-Lipper Biophotonics Center, Albert Einstein College of Medicine, Bronx, New York, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

21804536

Citation

Subach, Oksana M., et al. "A Photoswitchable Orange-to-far-red Fluorescent Protein, PSmOrange." Nature Methods, vol. 8, no. 9, 2011, pp. 771-7.
Subach OM, Patterson GH, Ting LM, et al. A photoswitchable orange-to-far-red fluorescent protein, PSmOrange. Nat Methods. 2011;8(9):771-7.
Subach, O. M., Patterson, G. H., Ting, L. M., Wang, Y., Condeelis, J. S., & Verkhusha, V. V. (2011). A photoswitchable orange-to-far-red fluorescent protein, PSmOrange. Nature Methods, 8(9), pp. 771-7. doi:10.1038/nmeth.1664.
Subach OM, et al. A Photoswitchable Orange-to-far-red Fluorescent Protein, PSmOrange. Nat Methods. 2011 Jul 31;8(9):771-7. PubMed PMID: 21804536.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A photoswitchable orange-to-far-red fluorescent protein, PSmOrange. AU - Subach,Oksana M, AU - Patterson,George H, AU - Ting,Li-Min, AU - Wang,Yarong, AU - Condeelis,John S, AU - Verkhusha,Vladislav V, Y1 - 2011/07/31/ PY - 2010/12/07/received PY - 2011/06/29/accepted PY - 2011/8/2/entrez PY - 2011/8/2/pubmed PY - 2011/11/1/medline SP - 771 EP - 7 JF - Nature methods JO - Nat. Methods VL - 8 IS - 9 N2 - We report a photoswitchable monomeric Orange (PSmOrange) protein that is initially orange (excitation, 548 nm; emission, 565 nm) but becomes far-red (excitation, 636 nm; emission, 662 nm) after irradiation with blue-green light. Compared to its parental orange proteins, PSmOrange has greater brightness, faster maturation, higher photoconversion contrast and better photostability. The red-shifted spectra of both forms of PSmOrange enable its simultaneous use with cyan-to-green photoswitchable proteins to study four intracellular populations. Photoconverted PSmOrange has, to our knowledge, the most far-red excitation peak of all GFP-like fluorescent proteins, provides diffraction-limited and super-resolution imaging in the far-red light range, is optimally excited with common red lasers, and can be photoconverted subcutaneously in a mouse. PSmOrange photoswitching occurs via a two-step photo-oxidation process, which causes cleavage of the polypeptide backbone. The far-red fluorescence of photoconverted PSmOrange results from a new chromophore containing N-acylimine with a co-planar carbon-oxygen double bond. SN - 1548-7105 UR - https://www.unboundmedicine.com/medline/citation/21804536/A_photoswitchable_orange_to_far_red_fluorescent_protein_PSmOrange_ L2 - http://dx.doi.org/10.1038/nmeth.1664 DB - PRIME DP - Unbound Medicine ER -