Thermodynamic effects of mutations on the denaturation of T4 lysozyme

18Citations
Citations of this article
19Readers
Mendeley users who have this article in their library.

Abstract

We investigated the folding of substantially destabilized mutant forms of T4 lysozyme using differential scanning calorimetry and circular dichroism measurements. Three mutations in an α-helix in the protein's N-terminal region, the alanine insertion mutations S44[A] and K48[A], and the substitution A42K had previously been observed to result in unexpectedly low apparent enthalpy changes of melting, compared to a pseudo-wild-type reference protein. The pseudo-wild-type reference protein thermally unfolds in an essentially two-state manner. However, we found that the unfolding of the three mutant proteins has a reduced cooperativity, which partially explains their lower apparent enthalpy changes. A three-state unfolding model including a discrete intermediate is necessary to describe the melting of the mutant proteins. The reduction in cooperativity must be considered for accurate calculation of the energy changes of folding. Unfolding in two stages reflects the underlying two-subdomain structure of the lysozyme protein family.

Cite

CITATION STYLE

APA

Carra, J. H., Murphy, E. C., & Privalov, P. L. (1996). Thermodynamic effects of mutations on the denaturation of T4 lysozyme. Biophysical Journal, 71(4), 1994–2001. https://doi.org/10.1016/S0006-3495(96)79397-9

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free