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5LZM
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BU of 5lzm by Molmil
COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Bell, J.A, Wilson, K, Zhang, X.-J, Faber, H.R, Nicholson, H, Matthews, B.W.
Deposit date:1991-01-25
Release date:1992-07-15
Last modified:2025-03-26
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths.
Proteins, 10, 1991
4A1X
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BU of 4a1x by Molmil
Co-Complex structure of NS3-4A protease with the inhibitory peptide CP5-46-A (Synchrotron data)
Descriptor: CHLORIDE ION, CP5-46-A PEPTIDE, NONSTRUCTURAL PROTEIN 4A, ...
Authors:Schmelz, S, Kuegler, J, Collins, J, Heinz, D.
Deposit date:2011-09-20
Release date:2012-09-19
Last modified:2024-10-16
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:High Affinity Peptide Inhibitors of the Hepatitis C Virus Ns3-4A Protease Refractory to Common Resistant Mutants.
J.Biol.Chem., 287, 2012
119L
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BU of 119l by Molmil
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
118L
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BU of 118l by Molmil
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
120L
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BU of 120l by Molmil
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
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BU of 122l by Molmil
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
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BU of 123l by Molmil
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
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BU of 125l by Molmil
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
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BU of 126l by Molmil
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
128L
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BU of 128l by Molmil
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
127L
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BU of 127l by Molmil
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
1L44
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BU of 1l44 by Molmil
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
Descriptor: T4 LYSOZYME
Authors:Daopin, S, Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2024-05-22
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability.
J.Mol.Biol., 221, 1991
1L58
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BU of 1l58 by Molmil
ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, T4 LYSOZYME
Authors:Nicholson, H, Matthews, B.W.
Deposit date:1991-05-06
Release date:1991-10-15
Last modified:2025-03-26
Method:X-RAY DIFFRACTION (1.65 Å)
Cite:
To be Published
1L71
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BU of 1l71 by Molmil
MULTIPLE STABILIZING ALANINE REPLACEMENTS WITHIN ALPHA-HELIX 126-134 OF T4 LYSOZYME HAVE INDEPENDENT, ADDITIVE EFFECTS ON BOTH STRUCTURE AND STABILITY
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME
Authors:Zhang, X, Matthews, B.W.
Deposit date:1991-09-23
Release date:1991-10-15
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability.
Protein Sci., 1, 1992
1L76
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BU of 1l76 by Molmil
TOLERANCE OF T4 LYSOZYME TO PROLINE SUBSTITUTIONS WITHIN THE LONG INTERDOMAIN ALPHA-HELIX ILLUSTRATES THE ADAPTABILITY OF PROTEINS TO POTENTIALLY DESTABILIZING LESIONS
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME
Authors:Sauer, U, Matthews, B.W.
Deposit date:1991-09-23
Release date:1991-10-15
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions.
J.Biol.Chem., 267, 1992
1L63
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BU of 1l63 by Molmil
ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME
Authors:Nicholson, H, Matthews, B.W.
Deposit date:1991-05-06
Release date:1991-10-15
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.75 Å)
Cite:Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme.
Biochemistry, 30, 1991
1L89
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BU of 1l89 by Molmil
SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Eriksson, A.E, Matthews, B.W.
Deposit date:1992-01-21
Release date:1993-10-31
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences.
J.Mol.Biol., 229, 1993
1L36
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BU of 1l36 by Molmil
TOWARD A SIMPLIFICATION OF THE PROTEIN FOLDING PROBLEM: A STABILIZING POLYALANINE ALPHA-HELIX ENGINEERED IN T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME
Authors:Zhang, X.-J, Baase, W.A, Matthews, B.W.
Deposit date:1990-12-26
Release date:1991-10-15
Last modified:2022-11-23
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme.
Biochemistry, 30, 1991
1L52
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BU of 1l52 by Molmil
STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME
Descriptor: T4 LYSOZYME
Authors:Daopin, S, Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2024-05-22
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme.
J.Mol.Biol., 221, 1991
1L40
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BU of 1l40 by Molmil
CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS
Descriptor: T4 LYSOZYME
Authors:Daopin, S, Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2024-05-22
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis.
Biochemistry, 30, 1991
1L47
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BU of 1l47 by Molmil
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
Descriptor: T4 LYSOZYME
Authors:Daopin, S, Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2024-05-22
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability.
J.Mol.Biol., 221, 1991
1L50
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BU of 1l50 by Molmil
STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME
Descriptor: T4 LYSOZYME
Authors:Daopin, S, Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2024-05-22
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme.
J.Mol.Biol., 221, 1991
1L38
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BU of 1l38 by Molmil
CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS
Descriptor: T4 LYSOZYME
Authors:Daopin, S, Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2024-05-22
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis.
Biochemistry, 30, 1991
1L45
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BU of 1l45 by Molmil
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
Descriptor: T4 LYSOZYME
Authors:Daopin, S, Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2024-05-22
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability.
J.Mol.Biol., 221, 1991
1L55
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BU of 1l55 by Molmil
ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME
Authors:Nicholson, H, Matthews, B.W.
Deposit date:1991-05-06
Release date:1991-10-15
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme.
Biochemistry, 30, 1991

238582

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