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A specific temperature-dependent conformational transition of hen egg-white lysozyme, occurring between 20 degree C and 30 degree C in solution, has been detected by 13-C-nuclear magnetic resonance spectroscopy. Selective changes in the chemical shifts of aromatic residues, together with differences in the chemical shifts, and nuclear Overhauser enhancement in the carbonyl, carboxyl, and alpha-carbon regions of the spectrum point to the vicinity of subsites D and E as the primary locus of the structural change.

Detection of new temperature-dependent conformational transition in lysozyme by carbon-13 nuclear magnetic resonance spectroscopy.