Abstract
The human immunodeficiency virus (HIV) is an enveloped RNA virus. Its inner core is composed of an RNP complex surrounded by a protein shell consisting of the capsid protein p24. Processes of assembly or disassembly of p24 are involved in the maturation and in the life cycle of the virus. Little structural information has been reported for HIV-1 p24. The availability of a recombinant variant of HIV-1 p24 (rp24) enabled studies on its conformation and conformational stability using circular dichroism (CD), fluorescence measurements and differential scanning calorimetry (DSC). The recombinant protein rp24 is composed of 234 amino acids, has a molecular mass of 25862 Da and differs at the N-terminus in five positions from the wild-type sequence [1].
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Hausdorf, G., Gewieß, A., Wray, V. and Porstmann, T., J. Virol. Methods, in press
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© 1995 Springer Science+Business Media Dordrecht
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Misselwitz, R., Hausdorf, G., Welfle, K., Höhne, W.E., Welfle, H. (1995). Conformation and Stability of Recombinant HIV-1 Capsid Protein P24 (rp24). In: Merlin, J.C., Turrell, S., Huvenne, J.P. (eds) Spectroscopy of Biological Molecules. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-0371-8_46
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DOI: https://doi.org/10.1007/978-94-011-0371-8_46
Publisher Name: Springer, Dordrecht
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