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
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 or Abstract |
|---|---|
| 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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