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102L	HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Heinz, D.W, Matthews, B.W. Deposit date: 1992-09-29 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.74 Å) Cite: How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme. Nature, 361, 1993
103L	HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Heinz, D.W, Matthews, B.W. Deposit date: 1992-09-29 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.9 Å) Cite: How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme. Nature, 361, 1993
104L	HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME Descriptor: T4 LYSOZYME Authors: Heinz, D.W, Matthews, B.W. Deposit date: 1992-09-29 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (2.8 Å) Cite: How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme. Nature, 361, 1993
107L	STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1992-12-17 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Structural basis of amino acid alpha helix propensity. Science, 260, 1993
108L	STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1992-12-17 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Structural basis of amino acid alpha helix propensity. Science, 260, 1993
109L	STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1992-12-17 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.85 Å) Cite: Structural basis of amino acid alpha helix propensity. Science, 260, 1993
110L	STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1992-12-17 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.7 Å) Cite: Structural basis of amino acid alpha helix propensity. Science, 260, 1993
111L	STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Descriptor: CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1992-12-17 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Structural basis of amino acid alpha helix propensity. Science, 260, 1993
112L	STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1992-12-17 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Structural basis of amino acid alpha helix propensity. Science, 260, 1993
113L	STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1992-12-17 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Structural basis of amino acid alpha helix propensity. Science, 260, 1993
114L	STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1992-12-17 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Structural basis of amino acid alpha helix propensity. Science, 260, 1993
115L	STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1992-12-17 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Structural basis of amino acid alpha helix propensity. Science, 260, 1993
118L	THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1993-05-28 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. Biochemistry, 32, 1993
119L	THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1993-05-28 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.65 Å) Cite: Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. Biochemistry, 32, 1993
120L	THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1993-05-28 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. Biochemistry, 32, 1993
122L	THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1993-05-28 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. Biochemistry, 32, 1993
123L	THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1993-05-28 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. Biochemistry, 32, 1993
125L	THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1993-05-28 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.85 Å) Cite: Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. Biochemistry, 32, 1993
126L	THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1993-05-28 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. Biochemistry, 32, 1993
127L	THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1993-05-28 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.85 Å) Cite: Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. Biochemistry, 32, 1993
128L	THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1993-05-28 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.7 Å) Cite: Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. Biochemistry, 32, 1993
129L	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
130L	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
131L	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
137L	STRUCTURAL BASIS OF AMINO ACID ALPHA HELIX PROPENSITY Descriptor: T4 LYSOZYME Authors: Blaber, M, Matthews, B.W. Deposit date: 1993-08-17 Release date: 1994-07-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.85 Å) Cite: Structural basis of amino acid alpha helix propensity. Science, 260, 1993

 

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