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

Authors :: Van Gilst M
Rees WA
von Hippel PH
Source :: Nucleic acids symposium series [Nucleic Acids Symp Ser] 1995 (33), pp. 145-7.
Publication Year :: 1995
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.

Subjects :: Bacteriophage lambda genetics
Bacteriophage lambda metabolism
Base Sequence
Binding Sites
Molecular Sequence Data
Molecular Structure
Nucleic Acid Conformation
Protein Binding
RNA, Viral genetics
Thermodynamics
Viral Regulatory and Accessory Proteins chemistry
RNA, Viral chemistry
RNA, Viral metabolism
Viral Regulatory and Accessory Proteins metabolism

Tools