Enhancement of Single-Molecule Fluorescence Signals by Colloidal Silver Nanoparticles in Studies of Protein Translation
Source abstract
Abstract
Metal-enhanced fluorescence (MEF) increased total photon emission of Cy3- and Cy5-labeled ribosomal initiation complexes near 50 nm silver particles 4- and 5.5-fold, respectively. Fluorescence intensity fluctuations above shot noise, at 0.1-5 Hz, were greater on silver particles. Overall signal-to-noise ratio was similar or slightly improved near the particles. Proximity to silver particles did not compromise ribosome function, as measured by codon-dependent binding of fluorescent tRNA, dynamics of fluorescence resonance energy transfer between adjacent tRNAs in the ribosome, and tRNA translocation induced by elongation factor G.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Advanced biosensing and bioanalysis techniques · RNA and protein synthesis mechanisms · Molecular Junctions and Nanostructures
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Department of Molecular Biology and Immunology, UNTHSC, Fort Worth, Texas 76107, United States
Pennsylvania Muscle Institute, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States
Anima Cell Metrology, Inc., Bernardsville, New Jersey 07924, United States
Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States
Department of Microbiology and Molecular Genetics, UMDNJ, Newark, New Jersey 07101, United States
References (51)
Show source-provided references
1. Lakowicz J. R. · 200610.1007/978-0-387-46312-4 ↗
2. Mason W. · 1999
3. Kapanidis A. N. · Trends Biochem. Sci. · 2009 · 34 · 23410.1016/j.tibs.2009.01.008 ↗
4. Aleman E. A. · Curr. Opin. Chem. Biol. · 2008 · 12 · 64710.1016/j.cbpa.2008.09.010 ↗
5. Deniz A. A. · J. R. Soc. Interface · 2008 · 5 · 1510.1098/rsif.2007.1021 ↗
6. Peters R. · Annu. Rev. Biophys. Biomol. Struct. · 2007 · 36 · 37110.1146/annurev.biophys.36.040306.132715 ↗
7. Bustamante C. · Nature · 2003 · 421 · 42310.1038/nature01405 ↗
8. Beausang J. F. · 2008 · 121
9. Peterman E. J. G. · Annu. Rev. Phys. Chem. · 2004 · 55 · 7910.1146/annurev.physchem.55.091602.094340 ↗
10. Goldman Y. E. · 2009 · 41
11. Ross J. L. · Nat. Cell Biol. · 2006 · 8 · 56210.1038/ncb1421 ↗
12. Sun Y. · Mol. Cell · 2007 · 28 · 95410.1016/j.molcel.2007.10.029 ↗
13. Dixit R. · Science · 2008 · 319 · 108610.1126/science.1152993 ↗
14. Galburt E. A. · Methods · 2009 · 48 · 32310.1016/j.ymeth.2009.04.021 ↗
15. Davenport R. J. · Science · 2000 · 287 · 249710.1126/science.287.5462.2497 ↗
16. Blanchard S. C. · Curr. Opin. Struct. Biol. · 2009 · 19 · 10310.1016/j.sbi.2009.01.002 ↗
17. Vanzi F. · Biophys. J. · 2005 · 89 · 190910.1529/biophysj.104.056283 ↗
18. Wang Y. · Biochemistry · 2007 · 46 · 1076710.1021/bi700657d ↗
19. Resch-Genger U. · Nat. Methods · 2008 · 5 · 76310.1038/nmeth.1248 ↗
20. Shaner N. C. · Nat. Methods · 2005 · 2 · 90510.1038/nmeth819 ↗
21. Miyawaki A. · Nat. Cell Biol. · 2003 · S1
22. Weiss S. · Science · 1999 · 283 · 167610.1126/science.283.5408.1676 ↗
23. Gell C. · 200610.1093/oso/9780198529422.001.0001 ↗
24. Lee S. F. · Chemphyschem. · 2009 · 10 · 217410.1002/cphc.200900200 ↗
25. Eid J. · Science · 2009 · 323 · 13310.1126/science.1162986 ↗
26. Aslan K. · Curr. Opin. Biotechnol. · 2005 · 16 · 5510.1016/j.copbio.2005.01.001 ↗
27. Lakowicz J. R. · Anal. Biochem. · 2005 · 337 · 17110.1016/j.ab.2004.11.026 ↗
28. Lakowicz J. R. · Anal. Biochem. · 2001 · 298 · 110.1006/abio.2001.5377 ↗
29. Ghosh S. K. · Chem. Rev. · 2007 · 107 · 479710.1021/cr0680282 ↗
30. Malicka J. · Anal. Biochem. · 2003 · 317 · 13610.1016/S0003-2697(03)00005-8 ↗
31. Fu Y. · Plasmonics · 2007 · 2 · 110.1007/s11468-007-9023-1 ↗
32. Mandecki W. · Proc. Soc. Photo. Opt. Instrum. Eng. · 2008 · 6862 · 68620T-1
33. Zhang J. · Anal. Chem. · 2009 · 81 · 88310.1021/ac801932m ↗
34. Govorov A. O. · Nano Lett. · 2007 · 7 · 62010.1021/nl062528t ↗
35. Kreibig U. · 1994
36. Peyser L. A. · Science · 2001 · 291 · 10310.1126/science.291.5501.103 ↗
37. Geddes C. D. · J. Phys. Chem. B. · 2003 · 18 · 998910.1021/jp030290g ↗
38. Moazed D. · Nature · 1989 · 342 · 14210.1038/342142a0 ↗
39. Agirrezabala X. · Mol. Cell · 2008 · 32 · 19010.1016/j.molcel.2008.10.001 ↗
40. Munro J. B. · Mol. Cell · 2007 · 25 · 50510.1016/j.molcel.2007.01.022 ↗
41. Blanchard S. C. · Proc. Natl. Acad. Sci. U.S.A. · 2004 · 101 · 1289310.1073/pnas.0403884101 ↗
42. Cooperman B. S. · FASEB J. · 2010 · 24 · 838-310.1096/fasebj.24.1_supplement.838.3 ↗
43. Pan D. · RNA · 2009 · 15 · 34610.1261/rna.1257509 ↗
44. Quinlan M. E. · Biophys. J. · 2005 · 89 · 113210.1529/biophysj.104.053496 ↗
45. Malicka J. · Anal. Biochem. · 2003 · 315 · 5710.1016/S0003-2697(02)00702-9 ↗
46. Lukomska J. · Biopolymers · 2006 · 81 · 24910.1002/bip.20407 ↗
47. Kapanidis A. N. · Acc. Chem. Res. · 2005 · 38 · 52310.1021/ar0401348 ↗
48. Sabanayagam C. R. · Appl. Phys. Lett. · 2004 · 84 · 121610.1063/1.1646725 ↗
49. Ha T. J. · Proc. Natl. Acad. Sci. U.S.A. · 1999 · 96 · 89310.1073/pnas.96.3.893 ↗
50. Robbins M. S. · IEEE Trans. Electron Devices · 2003 · 50 · 122710.1109/TED.2003.813462 ↗
51. McKinney S. A. · Biophys. J. · 2006 · 91 · 194110.1529/biophysj.106.082487 ↗