Fluorescence anisotropy of tyrosine using one-and two-photon excitation

Joseph R. Lakowicz; Borys Kierdaszuk; Patrik Callis; Henryk Malak; Ignacy Gryczynski

doi:10.1016/0301-4622(95)00040-5

Fluorescence anisotropy of tyrosine using one-and two-photon excitation

Joseph R. Lakowicz, Borys Kierdaszuk, Patrik Callis, Henryk Malak, Ignacy Gryczynski

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Abstract

We examined the emission spectra and steady-state anisotropy of tyrosyl fluorescence with two-photon excitation from 565 to 578 nm. The emission spectra of phenol and N-acetyl-l-tyrosinamide (NATyrA) were all the same for one-photon excitation (OPE) and two-photon excitation (TPE), and the tyrosine emission from ribonuclease A showed 10-nm shift to longer wavelengths with TPE. Surprisingly, the anisotropy of tyrosine, NATyrA and Leu⁵-enkephalin in frozen solution were near zero for TPE as compared to near 0.3 for OPE. Low values of the anisotropy near 0.05 were also found for phenol and ribonuclease A. A low anisotropy appears to be a basic characteristic of tyrosine or tyrosyl residues with two-photon excitation.

Original language	English
Pages (from-to)	263-271
Number of pages	9
Journal	Biophysical Chemistry
Volume	56
Issue number	3
DOIs	https://doi.org/10.1016/0301-4622(95)00040-5
State	Published - Nov 1995

Keywords

Anisotropy
Anisotropy spectra
Fluorescence
One-photon excitation
Peptides
Proteins
Tryptophan
Two-photon excitation
Tyrosine

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10.1016/0301-4622(95)00040-5

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@article{2900445c542641c6967cf2f1d4eb18ae,

title = "Fluorescence anisotropy of tyrosine using one-and two-photon excitation",

abstract = "We examined the emission spectra and steady-state anisotropy of tyrosyl fluorescence with two-photon excitation from 565 to 578 nm. The emission spectra of phenol and N-acetyl-l-tyrosinamide (NATyrA) were all the same for one-photon excitation (OPE) and two-photon excitation (TPE), and the tyrosine emission from ribonuclease A showed 10-nm shift to longer wavelengths with TPE. Surprisingly, the anisotropy of tyrosine, NATyrA and Leu5-enkephalin in frozen solution were near zero for TPE as compared to near 0.3 for OPE. Low values of the anisotropy near 0.05 were also found for phenol and ribonuclease A. A low anisotropy appears to be a basic characteristic of tyrosine or tyrosyl residues with two-photon excitation.",

keywords = "Anisotropy, Anisotropy spectra, Fluorescence, One-photon excitation, Peptides, Proteins, Tryptophan, Two-photon excitation, Tyrosine",

author = "Lakowicz, {Joseph R.} and Borys Kierdaszuk and Patrik Callis and Henryk Malak and Ignacy Gryczynski",

note = "Funding Information: This work was supported by grant RR-08 119 from National Institutes of Health; and by grant UM-141 from the Government Committee for Scientific Research (KBN, Poland). Dr. Borys Kierdaszuk is indebted to the Fulbright Scholar Program for Advanced Research Grant. PRC acknowledges support from NIH grant GM-3 1824.",

year = "1995",

month = nov,

doi = "10.1016/0301-4622(95)00040-5",

language = "English",

volume = "56",

pages = "263--271",

journal = "Biophysical Chemistry",

issn = "0301-4622",

publisher = "Elsevier",

number = "3",

}

TY - JOUR

T1 - Fluorescence anisotropy of tyrosine using one-and two-photon excitation

AU - Lakowicz, Joseph R.

AU - Kierdaszuk, Borys

AU - Callis, Patrik

AU - Malak, Henryk

AU - Gryczynski, Ignacy

N1 - Funding Information: This work was supported by grant RR-08 119 from National Institutes of Health; and by grant UM-141 from the Government Committee for Scientific Research (KBN, Poland). Dr. Borys Kierdaszuk is indebted to the Fulbright Scholar Program for Advanced Research Grant. PRC acknowledges support from NIH grant GM-3 1824.

PY - 1995/11

Y1 - 1995/11

N2 - We examined the emission spectra and steady-state anisotropy of tyrosyl fluorescence with two-photon excitation from 565 to 578 nm. The emission spectra of phenol and N-acetyl-l-tyrosinamide (NATyrA) were all the same for one-photon excitation (OPE) and two-photon excitation (TPE), and the tyrosine emission from ribonuclease A showed 10-nm shift to longer wavelengths with TPE. Surprisingly, the anisotropy of tyrosine, NATyrA and Leu5-enkephalin in frozen solution were near zero for TPE as compared to near 0.3 for OPE. Low values of the anisotropy near 0.05 were also found for phenol and ribonuclease A. A low anisotropy appears to be a basic characteristic of tyrosine or tyrosyl residues with two-photon excitation.

AB - We examined the emission spectra and steady-state anisotropy of tyrosyl fluorescence with two-photon excitation from 565 to 578 nm. The emission spectra of phenol and N-acetyl-l-tyrosinamide (NATyrA) were all the same for one-photon excitation (OPE) and two-photon excitation (TPE), and the tyrosine emission from ribonuclease A showed 10-nm shift to longer wavelengths with TPE. Surprisingly, the anisotropy of tyrosine, NATyrA and Leu5-enkephalin in frozen solution were near zero for TPE as compared to near 0.3 for OPE. Low values of the anisotropy near 0.05 were also found for phenol and ribonuclease A. A low anisotropy appears to be a basic characteristic of tyrosine or tyrosyl residues with two-photon excitation.

KW - Anisotropy

KW - Anisotropy spectra

KW - Fluorescence

KW - One-photon excitation

KW - Peptides

KW - Proteins

KW - Tryptophan

KW - Two-photon excitation

KW - Tyrosine

UR - http://www.scopus.com/inward/record.url?scp=0028840734&partnerID=8YFLogxK

U2 - 10.1016/0301-4622(95)00040-5

DO - 10.1016/0301-4622(95)00040-5

M3 - Article

C2 - 7578904

AN - SCOPUS:0028840734

SN - 0301-4622

VL - 56

SP - 263

EP - 271

JO - Biophysical Chemistry

JF - Biophysical Chemistry

IS - 3

ER -

Fluorescence anisotropy of tyrosine using one-and two-photon excitation

Abstract

Keywords

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