A nucleoprotein is any protein which is structurally associated with nucleic acid (either DNA or RNA). The prototypical example is any of the histone class of proteins, which are identifiable on strands of chromatin. Protamines are another class of nucleoproteins. A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... Highly simplified diagram of a double-stranded nucleic acid. ... Space-filling model of a section of DNA molecule Deoxyribonucleic acid (DNA) is a nucleic acid that contains the genetic instructions specifying the biological development of all cellular forms of life (and many viruses). ... Ribonucleic acid (RNA) is a nucleic acid consisting of a string of covalently-bound nucleotides. ... In biology, histones are the chief proteins of chromatin. ... Chromatin is the substance of a chromosome and consists of a complex of DNA and protein in eukaryotic cells. ... Protamine is a drug that reverses the anticoagulant effects of heparin by binding to it. ...
Although we were unable to isolate nucleoprotein in a single molecular form, nucleoprotein samples collected from the oligomeric peak fractions of a gel filtration column produced thin-plate crystals that diffract to 3.0 Å at synchrotron radiation sources.
The nucleoprotein crystal structure shows that a deep groove between the head and body domain, which is at the exterior of nucleoprotein oligomers, is probably the RNA-binding site (Figs 3b, d and 5).
At a nucleoprotein:RNA ratio of 1:1 and 2:1, 95% and 100% of the RNA, respectively, is bound to nucleoprotein (Supplementary Fig.
Nucleoprotein complexes were separated from unbound proteins by centrifugation, and proteins bound and those remaining free were analyzed by SDS-polyacrylamide gel electrophoresis (the image of the gel is simply an illustration of the expected results).
The stability of the nucleoprotein complexes was challenged by NaCl for 5 min at 37 °C. The amounts of Rad51 protein, Rad54 protein, and K341R Rad54 protein bound to ssDNA and dsDNA were determined using SDS-polyacrylamide gel electrophoresis.
The stability of the nucleoprotein complex was challenged by NaCl for 5 min at 37 °C. For each Rad54 protein concentration, the STMP was determined from experiments done at 5-11 different NaCl concentrations.
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