STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT

STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Pjura, P, Matthews, B.W. Deposit date: 1993-05-28 Release date: 1994-01-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.7 Å) Cite: Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent. Protein Sci., 2, 1993