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ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS[HYDROLASE(O-GLYCOSYL)]
View in iCn3D Similar StructuresPubMedProteinsConserved Domains
ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME[HYDROLASE]
View in iCn3D Similar StructuresPubMedProteinsConserved DomainsPubChem Compound
CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS[HYDROLASE]
BURIED POLAR MUTANT HUMAN LYSOZYME[HYDROLASE]
CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS[HYDROLASE]
T40A MUTANT HUMAN LYSOZYME[HYDROLASE]
CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME[HYDROLASE]
Crystal structure of Glu102-mutant human lysozyme doubly labeled with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine[HYDROLASE]
HUMAN LYSOZYME E102 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL GLYCOSIDE OF N-ACETYLLACTOSAMINE[HYDROLASE]
T43V MUTANT HUMAN LYSOZYME[HYDROLASE]
DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME[HYDROLASE (O-GLYCOSYL)]
CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V74A MUTANT[HYDROLASE (O-GLYCOSYL)]
CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V110A MUTANT[HYDROLASE (O-GLYCOSYL)]
ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS[HYDROLASE(O-GLYCOSYL)]
HUMAN LYSOZYME MUTANT WITH GLU 35 REPLACED BY ALA[LYSOZYME]
G68A HUMAN LYSOZYME[HYDROLASE]
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