Solution Structure by Site Directed Tryptophan Fluorescence in Tear Lipocalin

The solution structure of the G strand of human tear lipocalin was deduced by site directed tryptophan fluorescence (SDTF). The fluorescent amino acid, tryptophan, was sequentially substituted for each native amino acid in the sequence of the G strand. The fluorescent properties resolved alternating...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1997-10, Vol.239 (1), p.191-196
Main Authors: Gasymov, Oktay K., Abduragimov, Adil R., Yusifov, Taleh N., Glasgow, Ben J.
Format: Article
Language:English
Subjects:
Carrier Proteins - chemistry
Carrier Proteins - genetics
Circular Dichroism
Humans
Lipocalin 1
Mutagenesis, Site-Directed
Protein Structure, Secondary
Solutions
Spectrometry, Fluorescence
Tryptophan - chemistry
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Summary:The solution structure of the G strand of human tear lipocalin was deduced by site directed tryptophan fluorescence (SDTF). The fluorescent amino acid, tryptophan, was sequentially substituted for each native amino acid in the sequence of the G strand. The fluorescent properties resolved alternating periodicity as predicted for β sheet structure, twists in the β sheet, strand orientation in the lipocalin cavity, and the relative depth of residues in the cavity. A distribution of microstates with various orientations of dipoles in the side chain environments of the G strand revealed mobility on the nanosecond time scale. SDTF is broadly applicable to most proteins and will complement x-ray crystallography, site directed spin labeling by electron paramagnetic resonance (EPR), and nuclear magnetic resonance (NMR) in the determination of solution structure.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1997.7451