ArticleProtein science : a publication of the Protein Society1999
Global and local dynamics of the human U1A protein determined by tryptophan fluorescence.
Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 10 citations in OpenAlex.
- The role of the C-terminal helix of U1A protein in the interaction with U1hpII RNA.Nucleic acids research · 2013Article
- Characterization of the dynamics of an essential helix in the U1A protein by time-resolved fluorescence measurements.The journal of physical chemistry. B · 2008Article
- Chimeric peptide beacons: a direct polypeptide analog of DNA molecular beacons.Chemical communications (Cambridge, England) · 2007Article
- Peptide beacons: a new design for polypeptide-based optical biosensors.Bioconjugate chemistryArticle
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
Tryptophan residues have been introduced into two domains of the human U1A protein to probe solution dynamics. The full length protein contains 282 residues, separated into three distinct domains: the N-terminal RBD1 (RNA Binding Domain I), consisting of amino acids 1-101; the C-terminal RBD2, residues 202-282; and the intervening linker region. Tryptophan residues have been substituted for specific phenylalanine residues on the surface of the beta-sheet of either RBD1 or RBD2, thus introducing a single solvent exposed tryptophan as a fluorescence reporter. Both steady-state and time-resolved fluorescence measurements of the isolated RBD domains show that each tryptophan experiences a unique environment on the beta-sheet surface. The spectral properties of each tryptophan in RBD1 and RBD2 are preserved in the context of the U1A protein, indicating these domains do not interact with each other or with the linker region. The rotational correlation times of the isolated RBDs and the whole U1A, determined by dynamic polarization measurements, show that the linker region is highly flexible such that each RBD exhibits uncorrelated motion.
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