Document Detail


Measurement of subnanosecond anisotropy decays of protein fluorescence using frequency-domain fluorometry.
MedLine Citation:
PMID:  3944133     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We report the first anisotropy decays of protein fluorescence obtained using a frequency-domain fluorometer. The ultraviolet light source (300 nm) was a ring dye laser equipped with an intracavity frequency doubler, pumped by an argon ion laser. The data, measured at modulation frequencies from 2 to 200 MHz, reveal the presence of subnanosecond motions (0.1-0.2 ns) of the single tryptophan residues in melittin and monellin. For melittin the data also indicate the presence of slower motions near 1 ns, which may be the result of concerted motions of several peptide units. Smaller amplitude motions, on a similar timescale, were observed for the single tryptophan residue in staphylococcal nuclease. We demonstrate using N-acetyl-L-tryptophanamide in water that the method of frequency-domain fluorometry is capable of measuring correlation times as short as 50 ps. This method can provide data for the direct comparison of measured anisotropy decays with those predicted from molecular dynamics calculations.
Authors:
J R Lakowicz; G Laczko; I Gryczynski; H Cherek
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  261     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1986 Feb 
Date Detail:
Created Date:  1986-03-21     Completed Date:  1986-03-21     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2240-5     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Fluorescence*
Lasers
Protein Conformation
Proteins / analysis*
Rotation
Spectrometry, Fluorescence*
Time Factors
Grant Support
ID/Acronym/Agency:
GM 29318/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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