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Structural and thermodynamic characteristics of the binding of the lambda N protein to a RNA hairpin.

Van Gilst, M and Rees, W A and von Hippel, P H (1995) Structural and thermodynamic characteristics of the binding of the lambda N protein to a RNA hairpin. Nucleic acids symposium series (33). pp. 145-147. ISSN 0261-3166

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Abstract

The specific binding of the lambda N protein to a 15 nucleotide RNA oligomer that forms a hairpin structure has been investigated by biophysical methods. Using fluorescence spectroscopy and equilibrium ultra-centrifugation, it was found that the N protein binds specifically to this RNA hairpin as a monomer. Circular dichroism experiments show that both the N protein and the RNA hairpin undergo structural change upon association of the complex.

Item Type: Article
PubMed ID: 8643353
Keywords or MeSH Headings: Bacteriophage lambda/genetics/metabolism; Base Sequence; Binding Sites; Molecular Sequence Data; Molecular Structure; Nucleic Acid Conformation; Protein Binding; RNA, Viral/chemistry/genetics/metabolism; Thermodynamics; Viral Regulatory and Accessory Proteins/chemistry/metabolism;
Subjects: Molecules > RNA
Molecules > Molecular structure
Depositing User: Library Staff
Date Deposited: 24 Sep 2008 20:57
Last Modified: 21 May 2010 16:46
URI: http://authors.fhcrc.org/id/eprint/59

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