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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

1L49

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

1L54

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

1L68

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 (1.7 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

1L23

ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING
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:	Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc.Natl.Acad.Sci.USA, 84, 1987

1L43

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

1L61

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 (1.8 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

1L20

ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES
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 (1.85 Å)
Cite:	Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles. Nature, 336, 1988

1L29

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

1L53

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

1L66

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 (1.7 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

1L27

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 (1.8 Å)
Cite:	Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. Science, 239, 1988

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:	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

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

1L12

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
Descriptor:	T4 LYSOZYME
Authors:	Dao-Pin, S, Alber, T, Matthews, B.W.
Deposit date:	1988-02-05
Release date:	1988-04-16
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature, 330, 1987

1L03

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
Descriptor:	BETA-MERCAPTOETHANOL, 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:	Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature, 330, 1987

1L06

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
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:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature, 330, 1987

1L15

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
Descriptor:	T4 LYSOZYME
Authors:	Dao-Pin, S, Alber, T, Matthews, B.W.
Deposit date:	1988-02-05
Release date:	1988-04-16
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature, 330, 1987

1L13

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
Descriptor:	T4 LYSOZYME
Authors:	Dao-Pin, S, Alber, T, Matthews, B.W.
Deposit date:	1988-02-05
Release date:	1988-04-16
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature, 330, 1987

1L11

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
Descriptor:	BETA-MERCAPTOETHANOL, 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:	Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature, 330, 1987

1L14

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
Descriptor:	T4 LYSOZYME
Authors:	Dao-Pin, S, Alber, T, Matthews, B.W.
Deposit date:	1988-02-05
Release date:	1988-04-16
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature, 330, 1987

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