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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

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

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

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

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

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

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:	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

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:	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

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:	2022-11-23
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:	2022-11-23
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

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:	2022-11-23
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles. Nature, 336, 1988

1L22

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

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:	2022-11-23
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:	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

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:	2022-11-23
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

1T8A

USE OF SEQUENCE DUPLICATION TO ENGINEER A LIGAND-TRIGGERED LONG-DISTANCE MOLECULAR SWITCH IN T4 Lysozyme
Descriptor:	2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, GUANIDINE, ...
Authors:	Yousef, M.S, Baase, W.A, Matthews, B.W.
Deposit date:	2004-05-11
Release date:	2004-08-17
Last modified:	2024-02-14
Method:	X-RAY DIFFRACTION (2 Å)
Cite:	Use of sequence duplication to engineer a ligand-triggered, long-distance molecular switch in T4 lysozyme. Proc.Natl.Acad.Sci.USA, 101, 2004

1T97

Use of sequence duplication to engineer a ligand-triggered long-distance molecular switch in T4 Lysozyme
Descriptor:	Lysozyme
Authors:	Yousef, M.S, Baase, W.A, Matthews, B.W.
Deposit date:	2004-05-14
Release date:	2004-08-17
Last modified:	2024-02-14
Method:	X-RAY DIFFRACTION (2.7 Å)
Cite:	Use of sequence duplication to engineer a ligand-triggered, long-distance molecular switch in T4 lysozyme. Proc.Natl.Acad.Sci.USA, 101, 2004

1B6I

T4 LYSOZYME MUTANT WITH CYS 54 REPLACED BY THR, CYS 97 REPLACED BY ALA, THR 21 REPLACED BY CYS AND LYS 124 REPLACED BY CYS (C54T,C97A,T21C,K124C)
Descriptor:	2-HYDROXYETHYL DISULFIDE, PROTEIN (LYSOZYME)
Authors:	Vetter, I.R, Baase, W.A, Snow, S, Matthews, B.W.
Deposit date:	1999-01-14
Release date:	2000-01-12
Last modified:	2023-12-27
Method:	X-RAY DIFFRACTION (1.9 Å)
Cite:	Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme. Proc.Natl.Acad.Sci.USA, 97, 2000

119L

THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor:	BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:	Blaber, M, Matthews, B.W.
Deposit date:	1993-05-28
Release date:	1993-10-31
Last modified:	2024-02-07
Method:	X-RAY DIFFRACTION (1.65 Å)
Cite:	Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. Biochemistry, 32, 1993

118L

THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor:	BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:	Blaber, M, Matthews, B.W.
Deposit date:	1993-05-28
Release date:	1993-10-31
Last modified:	2024-02-07
Method:	X-RAY DIFFRACTION (1.8 Å)
Cite:	Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. Biochemistry, 32, 1993

120L

THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor:	BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:	Blaber, M, Matthews, B.W.
Deposit date:	1993-05-28
Release date:	1993-10-31
Last modified:	2024-02-07
Method:	X-RAY DIFFRACTION (1.8 Å)
Cite:	Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. Biochemistry, 32, 1993

123L

THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor:	BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:	Blaber, M, Matthews, B.W.
Deposit date:	1993-05-28
Release date:	1993-10-31
Last modified:	2024-02-07
Method:	X-RAY DIFFRACTION (1.8 Å)
Cite:	Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. Biochemistry, 32, 1993

125L

THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor:	BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:	Blaber, M, Matthews, B.W.
Deposit date:	1993-05-28
Release date:	1993-10-31
Last modified:	2024-02-07
Method:	X-RAY DIFFRACTION (1.85 Å)
Cite:	Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. Biochemistry, 32, 1993

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