Visible Fluorescence Spectroscopy of Single Proteins at Liquid-Helium Temperature

by: Satoru Fujiyoshi, Masanori Fujiwara, Michio Matsushita

Physical Review Letters, Vol. 100, No. 16. (2008)

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Abstract

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.

@article{citeulike:2759188, abstract = {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.}, author = {Fujiyoshi, Satoru and Fujiwara, Masanori and Matsushita, Michio }, citeulike-article-id = {2759188}, doi = {10.1103/PhysRevLett.100.168101}, journal = {Physical Review Letters}, keywords = {2008, biology, microscope, protein, structure, technique}, number = {16}, posted-at = {2008-05-05 22:00:21}, priority = {2}, publisher = {APS}, title = {Visible Fluorescence Spectroscopy of Single Proteins at Liquid-Helium Temperature}, url = {http://scitation.aip.org/getabs/servlet/GetabsServlet?prog=normal\&id=PRLTAO000100000016168101000001\&idtype=cvips\&gifs=yes}, volume = {100}, year = {2008} }

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TY - JOUR ID - citeulike:2759188 TI - Visible Fluorescence Spectroscopy of Single Proteins at Liquid-Helium Temperature JF - Physical Review Letters VL - 100 IS - 16 PB - APS N2 - 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. KW - 2008 KW - biology KW - microscope KW - protein KW - structure KW - technique AU - Fujiyoshi, Satoru AU - Fujiwara, Masanori AU - Matsushita, Michio PY - 2008/// UR - http://scitation.aip.org/getabs/servlet/GetabsServlet?prog=normal&id=PRLTAO000100000016168101000001&idtype=cvips&gifs=yes ER -

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