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1L36
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TOWARD A SIMPLIFICATION OF THE PROTEIN FOLDING PROBLEM: A STABILIZING POLYALANINE ALPHA-HELIX ENGINEERED IN T4 LYSOZYME
Descriptor:LYSOZYME, CHLORIDE ION, BETA-MERCAPTOETHANOL
Authors:Zhang, X.-J., Baase, W.A., Matthews, B.W.
Deposit date:1990-12-26
Release date:1991-10-15
Last modified:2017-11-29
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
1L37
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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:2017-11-29
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
1L38
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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:2017-11-29
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
1L39
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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:2017-11-29
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
1L40
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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:2017-11-29
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
1L41
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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:2017-11-29
Method:X-RAY DIFFRACTION (1.75 Å)
Cite:Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis.
Biochemistry, 30, 1991
1L42
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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:2017-11-29
Method:X-RAY DIFFRACTION (1.8 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
1L43
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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:2017-11-29
Method:X-RAY DIFFRACTION (1.8 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
1L44
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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:2017-11-29
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
1L45
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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:2017-11-29
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
1L46
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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:2017-11-29
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
1L47
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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:2017-11-29
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
1L48
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STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME
Descriptor:T4 LYSOZYME, BETA-MERCAPTOETHANOL
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
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
1L49
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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:2017-11-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme.
J.Mol.Biol., 221, 1991
1L50
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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:2017-11-29
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
1L51
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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:2017-11-29
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme.
J.Mol.Biol., 221, 1991
1L52
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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:2017-11-29
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
1L53
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STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME
Descriptor:T4 LYSOZYME, BETA-MERCAPTOETHANOL
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
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
1L54
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THE STRUCTURAL AND THERMODYNAMIC CONSEQUENCES OF BURYING A CHARGED RESIDUE WITHIN THE HYDROPHOBIC CORE OF T4 LYSOZYME
Descriptor:T4 LYSOZYME
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme.
Biochemistry, 30, 1991
1L55
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ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME
Descriptor:LYSOZYME, CHLORIDE ION, BETA-MERCAPTOETHANOL
Authors:Nicholson, H., Matthews, B.W.
Deposit date:1991-05-06
Release date:1991-10-15
Last modified:2017-11-29
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
1L56
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ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME
Descriptor:T4 LYSOZYME, BETA-MERCAPTOETHANOL
Authors:Nicholson, H., Matthews, B.W.
Deposit date:1991-05-06
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme.
Biopolymers, 32, 1992
1L57
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ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME
Descriptor:LYSOZYME, CHLORIDE ION, BETA-MERCAPTOETHANOL
Authors:Nicholson, H., Matthews, B.W.
Deposit date:1991-05-06
Release date:1991-10-15
Last modified:2017-11-29
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
1L58
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ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME
Descriptor:T4 LYSOZYME, BETA-MERCAPTOETHANOL
Authors:Nicholson, H., Matthews, B.W.
Deposit date:1991-05-06
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.65 Å)
Cite:
To be Published
1L59
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ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME
Descriptor:LYSOZYME, CHLORIDE ION, BETA-MERCAPTOETHANOL
Authors:Nicholson, H., Matthews, B.W.
Deposit date:1991-05-06
Release date:1991-10-15
Last modified:2017-11-29
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
1L60
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ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME
Descriptor:T4 LYSOZYME
Authors:Nicholson, H., Matthews, B.W.
Deposit date:1991-05-06
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme.
Biopolymers, 32, 1992
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