Issue

Vol. 32 No. 10 (2020): Vol 32 Issue 10

Copyright (c) 2020 AJC

Creative Commons License

This work is licensed under a Creative Commons Attribution 4.0 International License.

Study of Organization and Dynamics of Multi-Tryptophan Protein Molecules Utilizing Red Edge Excitation Shift Approach: A Review

https://doi.org/10.14233/ajchem.2020.22785
Anisur R. Molla
Department of Chemistry, Bidhannagar College, Salt Lake, Kolkata-700064, India
Pritha Mandal
Department of Chemistry, Krishnagar Government College, Krishnagar-741101, India

Corresponding Author(s) : Anisur R. Molla

anisur.chem@gmail.com

Asian Journal of Chemistry, Vol. 32 No. 10 (2020): Vol 32 Issue 10

Abstract

A shift in the fluorescence emission maxima with gradual increase in excitation wavelength is termed as red edge excitation shift (REES). Tryptophan residues are widely utilized as intrinsic fluorescence probe to investigate the protein structures. Wavelength selective tryptophan fluorescence can explore the dynamics of surrounded water molecules, the ubiquitous biological solvent. Thus REES experiment of various protein conformational states can provide significant input to the study of protein folding pathway and it can also be useful to study interaction of proteins with others. In this review article, we shall focus on red edge effect of various multi-tryptophan proteins in their respective native, intermediate and denatured state.

Keywords

Fluorescence Multi-tryptophan protein Red edge excitation shift Red edge effect Protein structure
R. Molla, A., & Mandal, P. (2020). Study of Organization and Dynamics of Multi-Tryptophan Protein Molecules Utilizing Red Edge Excitation Shift Approach: A Review. Asian Journal of Chemistry, 32(10), 2416–2422. https://doi.org/10.14233/ajchem.2020.22785
Download Citation
Endnote/Zotero/Mendeley (RIS)
BibTeX
References
  1. K. Henzler-Wildman and D. Kern, Nature, 450, 964 (2007);https://doi.org/10.1038/nature06522
  2. M.S. Smyth and J.H. Martin, Mol. Pathol., 53, 8 (2000); https://doi.org/10.1136/mp.53.1.8
  3. A. Chattopadhyay and S. Haldar, Acc. Chem. Res., 47, 12 (2014); https://doi.org/10.1021/ar400006z
  4. L. Anson, Nature, 459, 343 (2009); https://doi.org/10.1038/459343a
  5. J.R. Lakowicz, Principles of Fluorescence Spectroscopy, Kluwer-Plenum: New York (1999).
  6. A. Chattopadhyay and S. Mukherjee, J. Phys. Chem. B, 103, 8180 (1999); https://doi.org/10.1021/jp991303m
  7. A.P. Demchenko and A.S. Ladokhin, Eur. Biophys. J., 15, 369 (1988); https://doi.org/10.1007/BF00254724
  8. M. Taniguchi, H. Du and J.S. Lindsey, Photochem. Photobiol., 94,277 (2018); https://doi.org/10.1111/php.12862
  9. M. Taniguchi and J.S. Lindsey, Photochem. Photobiol., 94, 290 (2018); https://doi.org/10.1111/php.12860
  10. A.B.T. Ghisaidoobe and S.J. Chung, Int. J. Mol. Sci., 15, 22518 (2014); https://doi.org/10.3390/ijms151222518
  11. P.R. Callis, Methods Enzymol., 278, 113 (1997); https://doi.org/10.1016/S0076-6879(97)78009-1
  12. H. Raghuraman, D.A. Kelkar and A. Chattopadhyay, eds.: C.D. Geddes and J.R. Lakowicz, Novel Insights into Protein Structure and Dynamics Utilizing the Red Edge Excitation Shift, In: Reviews in Fluorescence, Springer: New York, pp 199-222 (2005).
  13. J.T. Vivian and P.R. Callis, Biophys. J., 80, 2093 (2001); https://doi.org/10.1016/S0006-3495(01)76183-8
  14. M.R. Eftink, ed.: C.H. Suelter, Fluorescence Techniques for Studying Protein Structure, In: Methods of Biochemical Analysis, John Wiley: New York, vol. 35, pp. 127-205 (1991).
  15. T. Nakano and A.L. Fink, J. Biol. Chem., 265, 12356 (1990).
  16. N. Tayeh, T. Rungassamy and J.R. Albani, J. Pharm. Biomed. Anal., 50, 107 (2009); https://doi.org/10.1016/j.jpba.2009.03.015
  17. P. Mandal, A.R. Molla and D.K. Mandal, J. Biochem., 154, 531 (2013); https://doi.org/10.1093/jb/mvt084
  18. A. Szabo, T. Stepanik, D. Wayner and N. Young, Biophys. J., 41, 233 (1983); https://doi.org/10.1016/S0006-3495(83)84433-6
  19. K.K. Rohatgi-Mukherjee, Fundamentals of Photochemistry, Wiley Eastern: New Delhi (1978).
  20. J.B. Birks, Photophysics of Aromatic Molecules, Wiley-Interscience: London (1970).
  21. K. Itoh and T. Azumi, J. Chem. Phys., 62, 3431 (1975); https://doi.org/10.1063/1.430977
  22. S.K. Cushing, M. Li, F. Huang and N. Wu, ACS Nano, 8, 1002 (2014); https://doi.org/10.1021/nn405843d
  23. J.R. Lakowicz and S. Keating-Nakamoto, Biochemistry, 23, 3013 (1984); https://doi.org/10.1021/bi00308a026
  24. S. Mukherjee and A. Chattopadhyay, Biochemistry, 33, 5089 (1994); https://doi.org/10.1021/bi00183a012
  25. A.P. Demchenko, Trends Biochem. Sci., 13, 374 (1988); https://doi.org/10.1016/0968-0004(88)90173-9
  26. A.P. Demchenko, Methods Enzymol., 450, 59 (2008); https://doi.org/10.1016/S0076-6879(08)03404-6
  27. S. Mukherjee and A. Chattopadhyay, J. Fluoresc., 5, 237 (1995); https://doi.org/10.1007/BF00723895
  28. A.P. Demchenko, Eur. Biophys. J., 16, 121 (1988); https://doi.org/10.1007/BF00255522
  29. D.W. Pierce and S.G. Boxer, Biophys. J., 68, 1583 (1995); https://doi.org/10.1016/S0006-3495(95)80331-0
  30. A.N. Rubinov and V.I. Tomin, Opt. Spectrosc. (USSR), 29, 1082 (1970).
  31. M.C. Galley and R.M. Purkey, Proc. Natl. Acad. Sci. USA, 67, 1116 (1970); https://doi.org/10.1073/pnas.67.3.1116
  32. A.P. Demchenko, Ukr. Biokhim. Zh., 53, 22 (1981).
  33. A.P. Demchenko, Luminescence and Dynamics of Protein Structure, Naukova Dumka: Kiev (1988).
  34. A.P. Demchenko, Luminescence, 17, 19 (2002); https://doi.org/10.1002/bio.671
  35. S. Guha, S.S. Rawat, A. Chattopadhyay and B. Bhattacharyya, Biochemistry, 35, 13426 (1996); https://doi.org/10.1021/bi961251g
  36. A.P. Demchenko, A.S. Ladokhin and E.G. Kostrzhevska, Mol. Biol. (Mosk.), 21, 663 (1987).
  37. Y.A.K. Reshetnyak and E.A. Burstein, Biofizika, 42, 293 (1997).
  38. J.M. Beechem and L. Brand, Annu. Rev. Biochem., 54, 43 (19 85);https://doi.org/10.1146/annurev.bi.54.070185.000355
  39. A.P. Demchenko, Ultraviolet Spectroscopy of Proteins, Springer-Verlag: Heidelberg, New York (1986).
  40. C. Slingsby and G.J. Wistow, Prog. Biophys. Mol. Biol., 115, 52 (2014); https://doi.org/10.1016/j.pbiomolbio.2014.02.006
  41. S.C. Rao and C.M. Rao, FEBS Lett., 337, 269 (1994); https://doi.org/10.1016/0014-5793(94)80206-8
  42. D.E. Fosket and L.C. Morejohn, Annu. Rev. Plant Physiol. Plant Mol. Biol., 43, 201 (1992); https://doi.org/10.1146/annurev.pp.43.060192.001221
  43. G.S. Gray and M. Kehoe, Infect. Immun., 46, 615 (1984); https://doi.org/10.1128/IAI.46.2.615-618.1984
  44. T.F. Spande and B. Witkop, Methods Enzymol., 11, 498 (1967); https://doi.org/10.1016/S0076-6879(67)11060-4
  45. S.M. Raja, S.S. Rawat, A. Chattopadhyay and A.K. Lala, Biophys. J.,76, 1469 (1999); https://doi.org/10.1016/S0006-3495(99)77307-8
  46. A. Chattopadhyay, S.S. Rawat, D.A. Kelkar, S. Ray and A. Chakrabarti, Protein Sci., 11, 2389 (2003); https://doi.org/10.1110/ps.03302003
  47. A. Chakrabarti, D.A. Kelkar and A. Chattopadhyay, Biosci. Rep., 26, 369 (2006); https://doi.org/10.1007/s10540-006-9024-x
  48. D.A. Kelkar, A. Chattopadhyay, A. Chakrabarti and M. Bhattacharyya, Biopolymers, 77, 325 (2005); https://doi.org/10.1002/bip.20233
  49. A.L. Fink, Annu. Rev. Biophys. Biomol. Struct., 24, 495 (1995); https://doi.org/10.1146/annurev.bb.24.060195.002431
  50. D.A. Kelkar, A. Chaudhuri, S. Haldar and A. Chattopadhyay, Eur. Biophys. J., 39, 1453 (2010); https://doi.org/10.1007/s00249-010-0603-1
  51. A. Chaudhuri, S. Haldar and A. Chattopadhyay, Biochem. Biophys. Res. Commun., 394, 1082 (2010); https://doi.org/10.1016/j.bbrc.2010.03.130
  52. H. Lis and N. Sharon, Chem. Rev., 98, 637 (1998); https://doi.org/10.1021/cr940413g
  53. F. Casset, T. Hamelryck, R. Loris, J.R. Brisson, C. Tellier, M.H. DaoThi, L. Wyns, F. Poortmans, S. Pérez and A. Imberty, J. Biol. Chem., 270, 25619 (1995); https://doi.org/10.1074/jbc.270.43.25619
  54. J.R. Albani, J. Fluoresc., 6, 199 (1996); https://doi.org/10.1007/BF00732823
  55. A.R. Molla, S.S. Maity, S. Ghosh and D.K. Mandal, Biochimie, 91,857 (2009); https://doi.org/10.1016/j.biochi.2009.04.006
  56. P. Mandal and D.K. Mandal, J. Fluoresc., 21, 2123 (2011); https://doi.org/10.1007/s10895-011-0913-4
  57. A. Chatterjee and D.K. Mandal, Biochim. Biophys. Acta, 1648, 174 (2003); https://doi.org/10.1016/S1570-9639(03)00120-1
  58. D. Sen and D.K. Mandal, Biochimie, 93, 409 (2011); https://doi.org/10.1016/j.biochi.2010.10.013
  59. A.R. Bizzarri and S. Cannistraro, J. Phys. Chem. B, 106, 6617 (2002); https://doi.org/10.1021/jp020100m
  60. C.Y. Wong and M.R. Eftink, Protein Sci., 6, 689 (1997); https://doi.org/10.1002/pro.5560060318
  61. M.K. Knight, R.E. Woolley, A. Kwok, S. Parsons, H.B.L. Jones, C.E. Gulácsy, P. Phaal, O. Kassaar, K. Dawkins, E. Rodriguez, A. Marques, L. Bowsher, S.A. Wells, A. Watts, J.M.H. van den Elsen, A. Turner, J. O’Hara and C.R. Pudney, bioRxiv 2020.03.23.003608; https://doi.org/10.1101/2020.03.23.003608
Read More
Author biographies is not available.
Download
PDF
Statistic
Read Counter : 1 Download : 2