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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

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:	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

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

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

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:	2024-05-22
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

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

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:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Nature, 334, 1988

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

1L16

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:	2024-05-22
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

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

1L18

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:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Nature, 334, 1988

1L32

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

1L67

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

1L07

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
Descriptor:	T4 LYSOZYME
Authors:	Dao-Pin, S, Faber, R, 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

1L08

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

1L19

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 (1.7 Å)
Cite:	Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles. Nature, 336, 1988

1L25

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

1L31

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

1L04

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

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

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

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

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