Abstract:
:The fluorescent properties of the amino acid tryptophan make it a useful tool for fluorometric assays. Because tryptophan fluorescence is remarkably sensitive to the polarity of the environment, it can be used to determine the affinity of tryptophan-containing peptides for phospholipid vesicles of varying compositions. Here, we describe a method for using tryptophan fluorescence to determine the binding affinities of peptides derived from the proteins Raf-1 and KSR-1 to small unilamellar vesicles containing phosphatidic acid. The method can be extrapolated to measure the binding of other tryptophan-containing peptides or proteins to lipid vesicles.
journal_name
Sci Signaljournal_title
Science signalingauthors
Kraft CA,Garrido JL,Leiva-Vega L,Romero Gdoi
10.1126/scisignal.299pl4subject
Has Abstractpub_date
2009-12-01 00:00:00pages
pl4issue
99eissn
1945-0877issn
1937-9145pii
scisignal.299pl4journal_volume
2pub_type
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