期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 114, 期 23, 页码 6005-6009出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1705586114
关键词
fluorescence protein; fluorescence probe; unnatural amino acid; imaging
资金
- National Institutes of Health (NIH) [P41-GM104605, GM54616]
- National Science Foundation Graduate Research Fellowship [DGE-1321851]
- NIH T32 Interdisciplinary Cardiovascular Training Grant [T32-HL007954]
Many fluorescent proteins are currently available for biological spectroscopy and imaging measurements, allowing a wide range of biochemical and biophysical processes and interactions to be studied at various length scales. However, in applications where a small fluorescence reporter is required or desirable, the choice of fluorophores is rather limited. As such, continued effort has been devoted to the development of amino acid-based fluorophores that do not require a specific environment and additional time to mature and have a large fluorescence quantum yield, long fluorescence lifetime, good photostability, and an emission spectrum in the visible region. Herein, we show that a tryptophan analog, 4-cyanotryptophan, which differs from tryptophan by only two atoms, is the smallest fluorescent amino acid that meets these requirements and has great potential to enable in vitro and in vivo spectroscopic and microscopic measurements of proteins.
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