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Thermodynamics of intersubunit interactions in cholera toxin upon binding to the oligosaccharide portion of its cell surface receptor, ganglioside GM1.
Schön A, Freire E. Schön A, et al. Among authors: freire e. Biochemistry. 1989 Jun 13;28(12):5019-24. doi: 10.1021/bi00438a017. Biochemistry. 1989. PMID: 2765522
Previously, we have shown that the association of cholera toxin to ganglioside GM1 enhances the cooperative interactions between subunits in the B-subunit pentamer [Goins, B., & Freire, E. (1988) Biochemistry 27, 2046-2052]. New experiments presented in this pap …
Previously, we have shown that the association of cholera toxin to ganglioside GM1 enhances the cooperative interactions between subunits in …
Molecular basis of cooperativity in protein folding. V. Thermodynamic and structural conditions for the stabilization of compact denatured states.
Xie D, Freire E. Xie D, et al. Among authors: freire e. Proteins. 1994 Aug;19(4):291-301. doi: 10.1002/prot.340190404. Proteins. 1994. PMID: 7984625

Recently is has been shown that alpha-lactalbumin at pH < 5 denatures into a molten globule state upon increasing the temperature (Griko, Y., Freire, E., Privalov, P.L. Biochemistry 33:1889-1899, 1994). This state has a lower heat capacity and a higher enthalpy a

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Recently is has been shown that alpha-lactalbumin at pH < 5 denatures into a molten globule state upon increasing the temperature (Griko,

…
The structural stability of the HIV-1 protease.
Todd MJ, Semo N, Freire E. Todd MJ, et al. Among authors: freire e. J Mol Biol. 1998 Oct 23;283(2):475-88. doi: 10.1006/jmbi.1998.2090. J Mol Biol. 1998. PMID: 9769219
447 results