help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

Biophysical Journal 51: 653-660 (1987)
© 1987 the Biophysical Society

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Janes, S M
Right arrow Articles by Hochstrasser, R M
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Janes, S M
Right arrow Articles by Hochstrasser, R M

Fluorescence and energy transfer of tryptophans in Aplysia myoglobin.

S M Janes, G Holtom, P Ascenzi, M Brunori and R M Hochstrasser

ABSTRACT

The fluorescence decay of tryptophan residues in apo and met Aplysia limacina myoglobin and sperm whale myoglobin were measured in aqueous solution at 10 degrees-15 degrees C. In all species, multiexponential behavior was observed in which the individual components displayed unique frequency-dependent emission characteristics. The results suggest that the tryptophan fluorescence in all met samples are quenched by rapid Forster energy transfer to the heme as predicted from the crystal geometry. Fluorescence from the apo protein is similar to that in solutions of free tryptophans. In addition, the fluorescence properties of the reversible thermal denaturation of Aplysia limacina met myoglobin was investigated between 25 degrees and 75 degrees C.




This article has been cited by other articles:


Home page
 Protein Sci.Home page
D. D. Castelli, E. Lovera, P. Ascenzi, and M. Fasano
Unfolding of the loggerhead sea turtle (Caretta caretta) myoglobin: A 1H-NMR and electronic absorbance study
Protein Sci., September 1, 2002; 11(9): 2273 - 2278.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Z. Gryczynski, J. Lubkowski, and E. Bucci
Heme-Protein Interactions in Horse Heart Myoglobin at Neutral pH and Exposed to Acid Investigated by Time-resolved Fluorescence in the Pico- to Nanosecond Time Range
J. Biol. Chem., August 18, 1995; 270(33): 19232 - 19237.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1987 by the Biophysical Society.