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PDB: 19 results
2TGI
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BU of 2tgi by Molmil
CRYSTAL STRUCTURE OF TRANSFORMING GROWTH FACTOR-BETA2: AN UNUSUAL FOLD FOR THE SUPERFAMILY
Descriptor: TRANSFORMING GROWTH FACTOR ,BETA 2
Authors:Daopin, S, Davies, D.R.
Deposit date:1993-10-20
Release date:1994-01-31
Last modified:2024-10-16
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily.
Science, 257, 1992
1L48
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BU of 1l48 by Molmil
STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, T4 LYSOZYME
Authors:Daopin, S, Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2022-11-23
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
1L51
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BU of 1l51 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 (1.9 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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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
1L53
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BU of 1l53 by Molmil
STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, T4 LYSOZYME
Authors:Daopin, S, Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2022-11-23
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
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
1L49
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BU of 1l49 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 (1.8 Å)
Cite:Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme.
J.Mol.Biol., 221, 1991
1L46
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BU of 1l46 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
1L42
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BU of 1l42 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 (1.8 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
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
1L37
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BU of 1l37 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
1L41
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BU of 1l41 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 (1.75 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
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
1L43
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BU of 1l43 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 (1.8 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
1L39
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BU of 1l39 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
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
1L54
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BU of 1l54 by Molmil
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:2024-05-22
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

227111

数据于2024-11-06公开中

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