Detection of new temperature-dependent conformational transition in lysozyme by carbon-13 nuclear magnetic resonance spectroscopy.
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.
D002247:Carbon Isotopes; D004529:Egg White; D009682:Magnetic Resonance Spectroscopy; D009113:Muramidase; D011487:Protein Conformation; D013696:Temperature; D014364:Tryptophan; D014443:Tyrosine
D002247:Carbon Isotopes; D014443:Tyrosine; D014364:Tryptophan; D009113:Muramidase