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Studies of the fluorescence of tyros...

Lee, Jinkeun.

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Studies of the fluorescence of tyrosine and tryptophan using trilinear analysis.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Studies of the fluorescence of tyrosine and tryptophan using trilinear analysis./
Author:	Lee, Jinkeun.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 1994,
Description:	176 p.
Notes:	Source: Dissertation Abstracts International, Volume: 56-01, Section: B, page: 1250.
Contained By:	Dissertation Abstracts International56-01B.
Subject:	Biophysics. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9517040

Studies of the fluorescence of tyrosine and tryptophan using trilinear analysis.
Lee, Jinkeun.

Studies of the fluorescence of tyrosine and tryptophan using trilinear analysis. - Ann Arbor : ProQuest Dissertations & Theses, 1994 - 176 p.

Source: Dissertation Abstracts International, Volume: 56-01, Section: B, page: 1250.

Thesis (Ph.D.)--The Ohio State University, 1994.

Tyrosine and tryptophan have been widely used as intrinsic probes for protein conformational studies. Better understanding of the fluorescence properties of these two fluorophores in different environments would make them more valuable intrinsic probes.Subjects--Topical Terms:

518360
Biophysics.

Studies of the fluorescence of tyrosine and tryptophan using trilinear analysis.
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008 180830s1994 ||||||||||||||||| ||eng d
035 $a (MiAaPQ)AAI9517040
035 $a AAI9517040
040 $a MiAaPQ $c MiAaPQ
100 1 $a Lee, Jinkeun. $3 3287757
245 1 0 $a Studies of the fluorescence of tyrosine and tryptophan using trilinear analysis.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 1994
300 $a 176 p.
500 $a Source: Dissertation Abstracts International, Volume: 56-01, Section: B, page: 1250.
500 $a Adviser: Robert T. Ross.
502 $a Thesis (Ph.D.)--The Ohio State University, 1994.
520 $a Tyrosine and tryptophan have been widely used as intrinsic probes for protein conformational studies. Better understanding of the fluorescence properties of these two fluorophores in different environments would make them more valuable intrinsic probes.
520 $a The characteristics of ligand binding of these fluorophores were studied using trilinear analysis. The fluorescence of any dilute specimen is separately linear in functions of each of the independent variables excitation wavelength, emission wavelength, and any treatment which alters concentration or fluorescence quantum yield. The resulting trilinear models have a structure that permits the mathematical dissection of spectra from complex specimens without the use of any other information about the properties of the specimen. Using this technique, the spectra of fluorophore:ligand complexes were resolved.
520 $a Ground-state hydrogen-bond complex formation was observed for both fluorophores. The origins of their emission are discussed in terms of hydrogen-bonded complexes for tyrosine, and exciplexes for tryptophan. The emission maximum wavelength of the hydrogen-bonded tyrosine shows a linear relationship with the pK$\sb{\rm a}$ of the ligand. The excitation spectral shift of hydrogen-bonded tyrosine is small except when the ligand is a model for the backbone carbonyl of a protein. The excitation spectral shift of hydrogen-bonded tyrosine was interpreted as the sum of the spectral shifts contributed by hydrogen-bonding with a proton acceptor (a red shift), hydrogen-bonding with a proton donor (a blue shift), and a dielectric effect (a blue shift). Complex formation between tryptophan and a ligand in a nonpolar environment causes a large red-shift in its emission spectrum. This complex formed in a nonpolar environment further red-shifts in a polar environment.
590 $a School code: 0168.
650 4 $a Biophysics. $3 518360
690 $a 0786
710 2 $a The Ohio State University. $3 718944
773 0 $t Dissertation Abstracts International $g 56-01B.
790 $a 0168
791 $a Ph.D.
792 $a 1994
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9517040