P10, A low molecular weight single-stranded nucleic acid-binding protein of murine leukemia retroviruses, shows stacking interactions of its single tryptophan residue with nucleotide bases
- 23 February 1988
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 27 (4) , 1172-1178
- https://doi.org/10.1021/bi00404a016
Abstract
Room temperature fluorescence and low-temperature phosphorescence studies of the association of p10, a basic low molecular weight single-stranded DNA binding protein isolated from murine leukemia viruses, point to the involvement of its single tryptophan residue in a close-range interaction with single-stranded polynucleotides. Optical detected triplet-state magnetic resonance (ODMR) techniques applied to the complex of p10 protein with the heavy atom derivatized polynucleotide poly(5-HgU) demonstrate the occurrence of stacking interactions of Trp35 with nucleic acid bases, thus agreeing with earlier reports that this residue is involved in the binding process process [Karpel, R. L., Henderson, L. E., and Oroszlan, S. (1987) J. Biol. Chem. 262, 4961-5967].This publication has 28 references indexed in Scilit:
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