THERMAL STABILITY DETERMINANTS OF CHICKEN EGG-WHITE LYSOZYME CORE MUTANTS: HYDROPHOBICITY, PACKING VOLUME AND CONSERVED BURIED WATER MOLECULES
Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules.
Structural and Thermodynamic Analysis of Compensating Mutations within the Core of Chicken Egg White Lysozyme
Ancestral Lysozymes Reconstructed, Neutrality Tested, and Thermostability Linked to Hydrocarbon Packing
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGLLQINSRWWCNDGRTPGSRNLCNIPC SALLSSDITATVNCAKKIVSSGNGMNAWVAWRNRCKGTDVQAWIRGCRL
STRUCTURAL DIFFERENCES BETWEEN WILDTYPE AND THE MUTANT MODELS ARE CONFINED TO THE REGION AROUND THE MUTATION (RESIDUE 91).
LYSOZYME (E.C.3.2.1.17) MUTANT WITH ILE 55 REPLACED BY LEU, SER 91 REPLACED BY THR, AND ASP 101 REPLACED BY SER (I55L,S91T,D101S)
MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRW WCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL