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1L32
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BU of 1l32 by Molmil
REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
Descriptor: T4 LYSOZYME
Authors:Bell, J.A, Dao-Pin, S, Matthews, B.W.
Deposit date:1989-05-01
Release date:1990-01-15
Last modified:2024-05-22
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.
Science, 239, 1988
1L33
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BU of 1l33 by Molmil
CONTRIBUTIONS OF LEFT-HANDED HELICAL RESIDUES TO THE STRUCTURE AND STABILITY OF BACTERIOPHAGE T4 LYSOZYME
Descriptor: T4 LYSOZYME
Authors:Nicholson, H, Matthews, B.W.
Deposit date:1989-05-01
Release date:1990-01-15
Last modified:2024-05-22
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme.
J.Mol.Biol., 210, 1989
1L34
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BU of 1l34 by Molmil
HIGH-RESOLUTION STRUCTURE OF THE TEMPERATURE-SENSITIVE MUTANT OF PHAGE LYSOZYME, ARG 96 (RIGHT ARROW) HIS
Descriptor: T4 LYSOZYME
Authors:Weaver, L.H, Matthews, B.W.
Deposit date:1989-05-01
Release date:1990-01-15
Last modified:2024-05-22
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:High-resolution structure of the temperature-sensitive mutant of phage lysozyme, Arg 96----His.
Biochemistry, 28, 1989
1L35
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BU of 1l35 by Molmil
STRUCTURE OF A THERMOSTABLE DISULFIDE-BRIDGE MUTANT OF PHAGE T4 LYSOZYME SHOWS THAT AN ENGINEERED CROSSLINK IN A FLEXIBLE REGION DOES NOT INCREASE THE RIGIDITY OF THE FOLDED PROTEIN
Descriptor: T4 LYSOZYME
Authors:Pjura, P.E, Matsumura, M, Wozniak, J.A, Matthews, B.W.
Deposit date:1989-10-26
Release date:1990-01-15
Last modified:2022-11-23
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein.
Biochemistry, 29, 1990
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
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: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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
1L56
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BU of 1l56 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: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

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