Metastable Aggregates in the Polymerisation of Tobacco-Mosaic-Virus Protein
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1977.tb11794.x/fullpdf
Reference40 articles.
1. 1. R. B. Scheele, T. M. Schuster, and L. H. Khairallah (1973 ) Abstr. 17th Ann. Meet. Biophys. Soc., p.290a .
2. Hysteresis of proton binding to tobacco mosaic virus protein associated with metastable polymerization
3. Tobacco mosaic virus protein: Kinetic and equilibrium studies on the pH-dependent transition A-protein→double disc
4. Kinetics of protein subunit interactions: Simulation of a polymerization overshoot
5. Structures and roles of the polymorphic forms of tobacco mosaic virus protein
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1. Dynamic mechanism of the self-assembly process of tobacco mosaic virus protein studied by rapid temperature-jump small-angle X-ray scattering using synchrotron radiation;Journal of Molecular Biology;1990-06
2. Temperature dependence of the structure of aggregates of tobacco mosaic virus protein at pH 7.2;Journal of Molecular Biology;1988-11
3. Neutral salt effects on the polymorphism of tobacco mosaic virus protein A contribution to the understanding of its mechanism of aggregation and virus reassembly;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1982-08
4. An EPR study of the kinetics of encapsidation of spin-labeled polyadenylic acid by TMV protein;FEBS Letters;1982-06-07
5. Scanning calorimetric investigation of the polymerization of the coat protein of tobacco mosaic virus;Biochemistry;1981-06-23
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