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STRUCTURAL ANALYSIS OF THE TEMPERATURE-SENSITIVE MUTANT OF BACTERIOPHAGE T4 LYSOZYME, GLYCINE 156 (RIGHT ARROW) ASPARTIC ACID
Descriptor:	T4 LYSOZYME
Authors:	Gray, T.M, Matthews, B.W.
Deposit date:	1988-02-05
Release date:	1988-04-16
Last modified:	2022-11-23
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Structural analysis of the temperature-sensitive mutant of bacteriophage T4 lysozyme, glycine 156----aspartic acid. J.Biol.Chem., 262, 1987

4LZM

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:	2024-02-28
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths. Proteins, 10, 1991

3LZM

STRUCTURAL STUDIES OF MUTANTS OF T4 LYSOZYME THAT ALTER HYDROPHOBIC STABILIZATION
Descriptor:	T4 LYSOZYME
Authors:	Wilson, K, Faber, R, Dao-Pin, S, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2022-11-23
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Structural studies of mutants of T4 lysozyme that alter hydrophobic stabilization. J.Biol.Chem., 264, 1989

5LZM

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:	2021-06-30
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

7LZM

COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS
Descriptor:	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:	2024-03-06
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

6LZM

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:	2021-06-30
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

1L34

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:	2022-11-23
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

1L26

REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
Descriptor:	BETA-MERCAPTOETHANOL, T4 LYSOZYME
Authors:	Bell, J.A, Dao-Pin, S, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2022-11-23
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

1L44

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:	2022-11-23
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

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 (1.65 Å)
Cite:	To be Published

1L64

TOLERANCE OF T4 LYSOZYME TO MULTIPLE XAA (RIGHT ARROW) ALA SUBSTITUTIONS: A POLYALANINE ALPHA-HELIX CONTAINING TEN CONSECUTIVE ALANINES
Descriptor:	BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME
Authors:	Heinz, D, 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:	Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. Proc.Natl.Acad.Sci.USA, 89, 1992

1L71

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

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

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

1L30

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:	2022-11-23
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

1L36

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

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:	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

1L10

STRUCTURAL STUDIES OF MUTANTS OF THE LYSOZYME OF BACTERIOPHAGE T4. THE TEMPERATURE-SENSITIVE MUTANT PROTEIN THR157 (RIGHT ARROW) ILE
Descriptor:	T4 LYSOZYME
Authors:	Dao-Pin, S, Wilson, K, Alber, T, Matthews, B.W.
Deposit date:	1988-02-05
Release date:	1988-04-16
Last modified:	2022-11-23
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157----Ile. J.Mol.Biol., 197, 1987

1L21

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:	2022-11-23
Method:	X-RAY DIFFRACTION (1.85 Å)
Cite:	Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. J.Mol.Biol., 210, 1989

1L28

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:	2022-11-23
Method:	X-RAY DIFFRACTION (1.9 Å)
Cite:	Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. Science, 239, 1988

1L40

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:	2022-11-23
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

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:	2022-11-23
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

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:	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

1L17

HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3
Descriptor:	T4 LYSOZYME
Authors:	Matsumura, M, Dao-Pin, S, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2022-11-23
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Nature, 334, 1988

1L33

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:	2022-11-23
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

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