Interaction lysozyme, thermodynamic

Hilser, V. J. Freire, E. (1996b). Structure based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors. J. Mol. Biol In Press. Hilser, V. J. Freire, E. (1996c). Structure-Based Statistical Thermodynamic Analysis of T4 Lysozyme Mutants Structural Mapping of Cooperative Interactions. Biophysical Chem.. ... 

Thermodynamic Parameters for Water Interacting with Lysozyme ... 

Selected examples of apparent free energies of interaction attributable to single amino acid side chains are summarized for three enzymes, T4 lysozyme, dihydrofolate reductase (DHFR), and tyrosyl-tRNA synthetase (TRS) (see Figs. 1,5, and 12, respectively, for structural information). In each case, the thermodynamic effect of the substitution was quantitated in terms of reduced binding affinity for the substrate or transition state, or reduced thermostability in the case of T4 lysozyme. 

Mann, G., Hermans, J. Modeling protein-small molecule interactions Structure and thermodynamics of noble gases binding in a cavity in mutant phage T4 lysozyme L99A, J. Mol. Biol. 2000, 302, 979-89. 

Martirosova, E. I. Regulation of hydrolase catalytic activity by alkylhydroxybenzenes thermodynamics of C-AHB and hen egg white lysozyme interaction. In Biotechnology and the Ecology of Big Cities. Nova Science Publishers N.-Y, 2011 105-113. 

The pH difference spectra of intact hen egg-white lysozyme and ester derivatives thereof have been measured at various ionic strengths and temperatures. The pH dependence of the extinction difference at 301.5 nm was well interpreted in terms of the ionization of the catalytic groups of L-aspartic acid 52 and L-glutamic acid 35 which interact electrostatically. The ionizations of these residues and the associated thermodynamic parameters were studied in detail. 

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