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ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS[HYDROLASE(O-GLYCOSYL)]
View in iCn3D Similar StructuresPubMedProteinsConserved Domains
ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS[HYDROLASE(O-GLYCOSYL)]
MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES[HYDROLASE]
CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME WITH FOUR EXTRA RESIDUES (EAEA) AT THE N-TERMINAL[HYDROLASE]
View in iCn3D Similar StructuresPubMedProteinsConserved DomainsPubChem Compound
CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS[HYDROLASE]
Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions[HYDROLASE]
CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS[HYDROLASE]
CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS[HYDROLASE]
ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME[HYDROLASE]
CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME[HYDROLASE]
CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY[HYDROLASE]
HUMAN LYSOZYME MUTANT WITH GLU 35 REPLACED BY ASP[HYDROLASE]
CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T[HYDROLASE]
BURIED POLAR MUTANT HUMAN LYSOZYME[HYDROLASE]
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