Phys. Rev. Lett. 100, 168101 (2008) [4 pages]Visible Fluorescence Spectroscopy of Single Proteins at Liquid-Helium TemperatureSee Also: Publisher's Note Received 16 August 2007; revised 18 December 2007; published 22 April 2008; corrected 24 April 2008 Fluorescence spectroscopy of single proteins at liquid-helium temperatures reveals a relation between structural dynamics and biological functions of the proteins. The technical difficulties in detecting visible fluorescence are chromatic aberration and optical background. They were overcome by a new optical design using reflective optics and employing two-photon excitation. The fluorescence spectrum of single green-fluorescent proteins taken at a temperature of 1.5 K makes a distinction between different metastable conformations that last for tens of seconds. © 2008 The American Physical Society URL:
http://link.aps.org/doi/10.1103/PhysRevLett.100.168101
DOI:
10.1103/PhysRevLett.100.168101
PACS:
87.15.−v, 82.37.Vb, 87.14.E−
See AlsoPublisher's Note: Satoru Fujiyoshi, Masanori Fujiwara, and Michio Matsushita, Publisher’s Note: Visible Fluorescence Spectroscopy of Single Proteins at Liquid-Helium Temperature [Phys. Rev. Lett. 100, 168101 (2008)], Phys. Rev. Lett. 100, 179903 (2008). |
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