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Erschienen in:
A Fluorescent Lifetime: Reminiscing About Gregorio Weber Kapitel lesen Erstes Kapitel lesen

2016 | OriginalPaper | Buchkapitel

Light Initiated Protein Relaxation

verfasst von : Ludwig Brand

Erschienen in: Perspectives on Fluorescence

Verlag: Springer International Publishing

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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.

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Vorheriges Kapitel Using Fluorescence to Characterize the Role of Protein Oligomerization in the Regulation of Gene Expression
Nächstes Kapitel Synthetic and Genetically Encoded Fluorescence Probes for Quantitative Analysis of Protein Hydrodynamics
Literatur
1.
Weber G (1961) Excited states of proteins. In: McElroy WD, Glass B (eds) Light and life. Johns Hopkins Press, Baltimore, pp 82–105
2.
Mataga N, Kaifu Y, Koizumi M (1956) Solvent effects upon fluorescence spectra and the dipole moments of excited molecules. Bull Chem Soc Jpn 29:465–470CrossRef
3.
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
4.
von Lippert E (1957) Spectroskopische bistimmung des dipolmomentes aromatischer verbndungen im ersten angeregten singulet tzustant. Z Electrochem 61:962–975
5.
Ross JBA, Schmidt CJ, Brand L (1981) Time resolved fluorescence of the two tryptophans in horse liver alcohol dehydrogenase. Biochemistry 20:4369–4377CrossRef
6.
Knutson JR, Walbridge DG, Brand L (1982) Decay-associated fluorescence spectra. Biochemistry 21:4671–4679CrossRef
7.
Knutson JR, Beechem JM, Brand L (1983) Simultaneous analysis of multiple fluorescence decay curves: a global approach. Chem Phys Lett 102:501–506CrossRef
8.
Daniel E, Weber G (1966) Cooperative effects in binding by bovine serum albumin. I. The binding of 1-anilino-8-naphthalenesufonate. Biochemistry 5:1893–1900CrossRef
9.
Stryer L (1965) The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: a fluorescent probe of non-polar binding sites. J Mol Biol 13:482–495CrossRef
10.
Weber G, Laurence DJR (1954) Fluorescent indicators of adsorption in aqueous solution and on the solid phase. Biochem J 56:xxxi
11.
Edelman GM, McClure WO (1968) Fluorescence probes and the conformation of proteins. Acc Chem Res 1:65
12.
Brand L, Gohlke JR (1971) Nanosecond time-resolved fluorescence spectra of a protein-dye complex. J Biol Chem 24:2317–2324
13.
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
14.
DeToma RP, Easter JH, Brand L (1976) Dynamic interactions of fluorescence probes with the solvent environment. J Am Chem Soc 98:6001–6007CrossRef
15.
DeToma RP, Brand L (1977) Excited-state solvation dynamics of 2-anilinonaphthalene. Chem Phys Lett 47:231–236CrossRef
16.
Gafni A, DeToma RP, Manrow RE, Brand L (1977) Nanosecond decay studies of a fluorescence probe bound to apomyoglobin. Biophys J 17:155–168CrossRef
17.
Toptygin D, Brand L (2000) Spectrally- and time-resolved fluorescence emission of indole during solvent relaxation: a quantitative model. Chem Phys Lett 322:496–502CrossRef
18.
Toptygin D, Savtchenko RS, Meadow ND, Brand L (2001) Homogeneous. J Phys Chem B 105:2043–2055CrossRef
19.
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 110:26292–26302CrossRef
20.
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 114:11323–11337CrossRef
21.
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 39:11216–11226CrossRef
22.
Cohen BE, McAnaney TB, Park ES, Jan YN, Boxer SC, Jan LY (2002) Probing protein electrostatics with a synthetic fluorescent amino acid. Science 396:1700–1703CrossRef
23.
Nilsson L, Halle B (2005) Molecular origin of time-dependent spectral shifts in proteins. Proc Natl Acad Sci U S A 102:13867–13872CrossRef
24.
Halle B, Nilsson L (2009) Does the dynamic shift report on slow protein hydration dynamics? J Phys Chem B Lett 113:8210–8213CrossRef
25.
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
26.
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
Metadaten
Titel
Light Initiated Protein Relaxation
verfasst von
Ludwig Brand
Copyright-Jahr
2016
Buch
Perspectives on Fluorescence

Print ISBN: 978-3-319-41326-6

Electronic ISBN: 978-3-319-41328-0

Copyright-Jahr: 2016

DOI
https://doi.org/10.1007/4243_2016_18

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