Abstract
Absorption of light by solvatochromic dyes including tryptophan leads to formation of an excited state with a change in the magnitude and/or direction of its permanent electric dipole moment. The excited state can interact with surrounding atoms with formation of a relaxed state. The kinetics of this process can be measured by time/energy-resolved fluorescence spectroscopy. Time-dependent spectral shifts (time-resolved emission spectra) provide information about protein relaxation. Ground-state heterogeneity, two-state excited-state reactions, and dielectric relaxation all give rise to time-dependent spectral shifts. Ways to tell these processes apart are discussed. Examples are presented which illustrate how rates and extent of spectral shifts can differentiate between ordered and disordered parts of a protein molecule. Rates of spectral shifts can be related to nanosecond motions of specific protein residues.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Similar content being viewed by others
References
Weber G (1961) Excited states of proteins. In: McElroy WD, Glass B (eds) Light and life. Johns Hopkins Press, Baltimore, pp 82–105
Mataga N, Kaifu Y, Koizumi M (1956) Solvent effects upon fluorescence spectra and the dipole moments of excited molecules. Bull Chem Soc Jpn 29:465–470
Bakhshiev NG (1961) Universal molecular interactions and their effect on the position of the electronic spectra of molecules in component solutions. I. Theory (Liquid solutions). Opt Spectrosc 10:379–384
von Lippert E (1957) Spectroskopische bistimmung des dipolmomentes aromatischer verbndungen im ersten angeregten singulet tzustant. Z Electrochem 61:962–975
Ross JBA, Schmidt CJ, Brand L (1981) Time resolved fluorescence of the two tryptophans in horse liver alcohol dehydrogenase. Biochemistry 20:4369–4377
Knutson JR, Walbridge DG, Brand L (1982) Decay-associated fluorescence spectra. Biochemistry 21:4671–4679
Knutson JR, Beechem JM, Brand L (1983) Simultaneous analysis of multiple fluorescence decay curves: a global approach. Chem Phys Lett 102:501–506
Daniel E, Weber G (1966) Cooperative effects in binding by bovine serum albumin. I. The binding of 1-anilino-8-naphthalenesufonate. Biochemistry 5:1893–1900
Stryer L (1965) The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: a fluorescent probe of non-polar binding sites. J Mol Biol 13:482–495
Weber G, Laurence DJR (1954) Fluorescent indicators of adsorption in aqueous solution and on the solid phase. Biochem J 56:xxxi
Edelman GM, McClure WO (1968) Fluorescence probes and the conformation of proteins. Acc Chem Res 1:65
Brand L, Gohlke JR (1971) Nanosecond time-resolved fluorescence spectra of a protein-dye complex. J Biol Chem 24:2317–2324
Bakhshiev NG, Mazurenko Yu. T, Piterskayer VI (1966) Luminescence decay in different portions of the luminescence spectrum of molecules in viscous solution. Opt Spectrosc 21:307–309
DeToma RP, Easter JH, Brand L (1976) Dynamic interactions of fluorescence probes with the solvent environment. J Am Chem Soc 98:6001–6007
DeToma RP, Brand L (1977) Excited-state solvation dynamics of 2-anilinonaphthalene. Chem Phys Lett 47:231–236
Gafni A, DeToma RP, Manrow RE, Brand L (1977) Nanosecond decay studies of a fluorescence probe bound to apomyoglobin. Biophys J 17:155–168
Toptygin D, Brand L (2000) Spectrally- and time-resolved fluorescence emission of indole during solvent relaxation: a quantitative model. Chem Phys Lett 322:496–502
Toptygin D, Savtchenko RS, Meadow ND, Brand L (2001) Homogeneous. J Phys Chem B 105:2043–2055
Toptygin D, Gronenborn AM, Brand L (2006) Nanosecond relaxation dynamics of protein GB1, by the time-dependent red shift in the fluorescence of tryptophan and 5-fluorotryptophan. J Phys Chem B 110:26292–26302
Toptygin D, Woolf TB, Brand L (2010) Picosecond protein dynamics: the origin of the time-dependent spectral shift in the fluorescence of the single trp in the protein GB1. J Phys Chem B 114:11323–11337
Tcherkasskaya O, Knutson JR, Bowley SA, Frank MA, Gronenborn A (2000) Nanosecond dynamics of the single tryptophan reveals multi-state equilibrium unfolding of protein GB1. Biochemistry 39:11216–11226
Cohen BE, McAnaney TB, Park ES, Jan YN, Boxer SC, Jan LY (2002) Probing protein electrostatics with a synthetic fluorescent amino acid. Science 396:1700–1703
Nilsson L, Halle B (2005) Molecular origin of time-dependent spectral shifts in proteins. Proc Natl Acad Sci U S A 102:13867–13872
Halle B, Nilsson L (2009) Does the dynamic shift report on slow protein hydration dynamics? J Phys Chem B Lett 113:8210–8213
Toptygin D (2014) Analysis of time-dependent red shifts in fluorescence emission from tryptophan residues in proteins (Ch 9). In: Engelborghs Y, Visser AJWG (eds) Fluorescence spectroscopy and microscopy: methods and protocols. Springer Science, pp 215–255
Toptygin D (2016) Time-dependent spectral shifts spectral shifts in tryptophan fluorescence: bridging experiments with molecular dynamics simulations (Ch 2). In: Geddes CD (ed) Reviews in fluorescence. Springer, pp 29–69
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2016 Springer International Publishing Switzerland
About this chapter
Cite this chapter
Brand, L. (2016). Light Initiated Protein Relaxation. In: Jameson, D. (eds) Perspectives on Fluorescence. Springer Series on Fluorescence, vol 17. Springer, Cham. https://doi.org/10.1007/4243_2016_18
Download citation
DOI: https://doi.org/10.1007/4243_2016_18
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-41326-6
Online ISBN: 978-3-319-41328-0
eBook Packages: Chemistry and Materials ScienceChemistry and Material Science (R0)