Abstract
A mean-field theoretical approach is applied to streptavidin tetramerization and two-dimensional (2D) crystallization. This theory includes, in particular, solvent-residue interactions following the inhomogeneous Flory-Huggins model for polymers. It also takes into account residue-residue interactions by using tabulated pair interaction parameters. This theory allows one to explicitly calculate the entropy of the inhomogeneous system. We show that hydrophobic interactions are responsible for the stability of tetramerization. Within the present theory, the equilibrium distance between the two dimers is the same as that determined experimentally. The free energy of tetramerization (i.e., dissociation of the two dimers) is 50 k(B)T. Unlike tetramerization, hydrophobic interactions alone are not sufficient to stabilize the 2D crystal C(222), but solvent-mediated residue-residue interactions give the most important contribution.
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- Chothia C., Janin J. Principles of protein-protein recognition. Nature. 1975 Aug 28;256(5520):705–708. doi: 10.1038/256705a0. [DOI] [PubMed] [Google Scholar]
- Durbin S. D., Feher G. Protein crystallization. Annu Rev Phys Chem. 1996;47:171–204. doi: 10.1146/annurev.physchem.47.1.171. [DOI] [PubMed] [Google Scholar]
- Eisenberg D., McLachlan A. D. Solvation energy in protein folding and binding. Nature. 1986 Jan 16;319(6050):199–203. doi: 10.1038/319199a0. [DOI] [PubMed] [Google Scholar]
- Katz B. A. Binding to protein targets of peptidic leads discovered by phage display: crystal structures of streptavidin-bound linear and cyclic peptide ligands containing the HPQ sequence. Biochemistry. 1995 Nov 28;34(47):15421–15429. doi: 10.1021/bi00047a005. [DOI] [PubMed] [Google Scholar]
- Lee B., Richards F. M. The interpretation of protein structures: estimation of static accessibility. J Mol Biol. 1971 Feb 14;55(3):379–400. doi: 10.1016/0022-2836(71)90324-x. [DOI] [PubMed] [Google Scholar]
- Noolandi J., Davison T. S., Volkel A. R., Nie X., Kay C., Arrowsmith C. H. A meanfield approach to the thermodynamics of a protein-solvent system with application to the oligomerization of the tumor suppressor p53. Proc Natl Acad Sci U S A. 2000 Aug 29;97(18):9955–9960. doi: 10.1073/pnas.160075697. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Olson M. A. Mean-field analysis of protein-protein interactions. Biophys Chem. 1998 Nov 16;75(2):115–128. doi: 10.1016/s0301-4622(98)00201-4. [DOI] [PubMed] [Google Scholar]
- Sano T., Vajda S., Smith C. L., Cantor C. R. Engineering subunit association of multisubunit proteins: a dimeric streptavidin. Proc Natl Acad Sci U S A. 1997 Jun 10;94(12):6153–6158. doi: 10.1073/pnas.94.12.6153. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Skolnick J., Jaroszewski L., Kolinski A., Godzik A. Derivation and testing of pair potentials for protein folding. When is the quasichemical approximation correct? Protein Sci. 1997 Mar;6(3):676–688. doi: 10.1002/pro.5560060317. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Young L., Jernigan R. L., Covell D. G. A role for surface hydrophobicity in protein-protein recognition. Protein Sci. 1994 May;3(5):717–729. doi: 10.1002/pro.5560030501. [DOI] [PMC free article] [PubMed] [Google Scholar]