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Calcium ion binding by tobacco mosaic virus
Journal of Molecular Biology
|November 15, 1983
Summary
Tobacco mosaic virus has two calcium ion binding sites per subunit. These sites show varying affinities and release hydrogen ions, influencing the virus particle
Area of Science:
- Biophysics
- Biochemistry
- Virology
Background:
- Tobacco mosaic virus (TMV) is a well-characterized plant virus.
- Understanding ion binding is crucial for viral stability and interactions.
Purpose of the Study:
- To quantify calcium ion binding to tobacco mosaic virus.
- To investigate the influence of pH and ionic strength on calcium binding.
Main Methods:
- Calcium ion titrations using a calcium-specific ion-exchange electrode.
- Scatchard analysis to determine binding site number and affinity.
- Experiments conducted in water and 0.01 M KCl solutions.
Main Results:
- TMV possesses two distinct calcium ion binding sites per protein subunit with high affinity (stability constants > 10(4) M-1).
- Calcium binding releases hydrogen ions, with up to two H+ released per Ca2+ at higher affinity sites in water.
- Apparent stability constants and hydrogen ion release vary with pH and ionic strength.
Conclusions:
- The electrical charge on the TMV particle may remain relatively constant across a pH range despite expected variations.
- Independent titration of two non-identical binding sites explains observed calcium-ion interactions.
- These findings provide insights into the electrostatic properties and ion-binding behavior of TMV.