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Titolo:
SITE-TO-SITE DIFFUSION IN PROTEINS AS OBSERVED BY ENERGY-TRANSFER ANDFREQUENCY-DOMAIN FLUOROMETRY
Autore:
LAKOWICZ JR; GRYCZYNSKI I; KUSBA J; WICZK W; SZMACINSKI H; JOHNSON ML;
Indirizzi:
UNIV MARYLAND,SCH MED,CTR FLUORESCENCE SPECT,DEPT BIOL CHEM,108 N GREENE ST BALTIMORE MD 21201 UNIV VIRGINIA,DEPT PHARMACOL CHARLOTTESVILLE VA 22908
Titolo Testata:
Photochemistry and photobiology
fascicolo: 1, volume: 59, anno: 1994,
pagine: 16 - 29
SICI:
0031-8655(1994)59:1<16:SDIPAO>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
END DISTANCE DISTRIBUTIONS; TIME-RESOLVED FLUORESCENCE; FLEXIBLE MOLECULES; EXCITATION-ENERGY; FORSTER DISTANCE; TROPONIN-I; RESOLUTION; DYNAMICS; DECAY; COEFFICIENTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
74
Recensione:
Indirizzi per estratti:
Citazione:
J.R. Lakowicz et al., "SITE-TO-SITE DIFFUSION IN PROTEINS AS OBSERVED BY ENERGY-TRANSFER ANDFREQUENCY-DOMAIN FLUOROMETRY", Photochemistry and photobiology, 59(1), 1994, pp. 16-29

Abstract

We report measurements of the site-to-site diffusion coefficients in proteins and model compounds, which were measured using time-dependentenergy transfer and frequency-domain fluorometry. The possibility of measuring these diffusion coefficients were shown from simulations, which demonstrate that donor (D)-to-acceptor (A) diffusion alters the donor frequency response, and that this effect is observable in the presence of a distribution of donor-to-acceptor distances. For decay timestypical of tryptophan fluorescence, the simulations indicate that D-Adiffusion coefficients can be measured ranging from 10(-7) to 10(-5) cm(2)/s. This possibility was verified by studies of a methylene-chainlinked D-A pair in solutions of varying viscosity. The D-A diffusion was also measured for two labeled peptides and two proteins, melittin and troponin I. In most cases we used global analysis of data sets obtained with varying amounts of collisional quenchers to vary the donor decay time. Unfolding of troponin I results in more rapid D-A diffusion, whereas for melittin more rapid diffusion was observed in the alpha-helical state but over a limited range of distances.

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Documento generato il 04/12/20 alle ore 16:17:15