Streak Camera Methods In Nucleic Acid And Protein Fluorescence Spectroscopy

1988 ◽  
Author(s):  
Thomas M. Nordlund
Keyword(s):  
Nucleic Acid ◽  
Fluorescence Spectroscopy ◽  
Streak Camera ◽  
Protein Fluorescence

Multidimensional fluorescence spectroscopy using a streak camera based pulse fluorometer

1998 ◽  
Vol 69 (3) ◽  
pp. 1512-1518 ◽  
Author(s):  
Christof A. Bühler ◽  
Urs Graf ◽  
Remo A. Hochstrasser ◽  
Max Anliker
Keyword(s):  
Fluorescence Spectroscopy ◽  
Streak Camera ◽  
Multidimensional Fluorescence

Picosecond fluorescence spectroscopy of purple membrane in Halobacterium halobium with a photon-counting streak camera

1990 ◽  
Vol 168 (5) ◽  
pp. 493-498 ◽  
Author(s):  
Hiroyuki Ohtani ◽  
Mitsuru Ishikawa ◽  
Hiroyasu Itoh ◽  
Yoshihiro Takiguchi ◽  
Tsuneyuki Urakami ◽  
...  
Keyword(s):  
Fluorescence Spectroscopy ◽  
Streak Camera ◽  
Photon Counting ◽  
Purple Membrane ◽  
Halobacterium Halobium

Time-resolved two-photon excited fluorescence spectroscopy based on a streak camera

2006 ◽  
Author(s):  
Lixin Liu ◽  
Junle Qu ◽  
Danni Chen ◽  
Ziyang Lin ◽  
Gaixia Xu ◽  
...  
Keyword(s):  
Fluorescence Spectroscopy ◽  
Streak Camera ◽  
Time Resolved ◽  
Two Photon

scholarly journals Crystal Structure of the YchF Protein Reveals Binding Sites for GTP and Nucleic Acid

2003 ◽  
Vol 185 (14) ◽  
pp. 4031-4037 ◽  
Author(s):  
Alexey Teplyakov ◽  
Galina Obmolova ◽  
Seung Y. Chu ◽  
John Toedt ◽  
Edward Eisenstein ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Nucleic Acid ◽  
Binding Site ◽  
Coiled Coil ◽  
Genomic Analysis ◽  
Protein Fluorescence ◽  
Terminal Domain ◽  
Fluorescence Measurements ◽  
Α Helix

ABSTRACT The bacterial protein encoded by the gene ychF is 1 of 11 universally conserved GTPases and the only one whose function is unknown. The crystal structure determination of YchF was sought to help with the functional assignment of the protein. The YchF protein from Haemophilus influenzae was cloned and expressed, and the crystal structure was determined at 2.4 Å resolution. The polypeptide chain is folded into three domains. The N-terminal domain has a mononucleotide binding fold typical for the P-loop NTPases. An 80-residue domain next to it has a pronounced α-helical coiled coil. The C-terminal domain features a six-stranded half-barrel that curves around an α-helix. The crablike three-domain structure of YchF suggests the binding site for a double-stranded nucleic acid in the cleft between the domains. The structure of the putative GTP-binding site is consistent with the postulated guanine specificity of the protein. Fluorescence measurements have demonstrated the ability of YchF to bind a double-stranded nucleic acid and GTP. Taken together with other experimental data and genomic analysis, these results suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translation factor.

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