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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
1L49
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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
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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
1L68
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BU of 1l68 by Molmil
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
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BU of 1l23 by Molmil
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
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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
1L26
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BU of 1l26 by Molmil
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
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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
1L58
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BU of 1l58 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 (1.65 Å)
Cite:
To be Published
1L64
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BU of 1l64 by Molmil
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
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BU of 1l71 by Molmil
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
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BU of 1l76 by Molmil
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
1L20
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BU of 1l20 by Molmil
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
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BU of 1l29 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
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
1L66
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BU of 1l66 by Molmil
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
177L
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BU of 177l by Molmil
Protein flexibility and adaptability seen in 25 crystal forms of T4 LYSOZYME
Descriptor: T4 LYSOZYME
Authors:Matsumura, M, Weaver, L, Zhang, X.-J, Matthews, B.W.
Deposit date:1995-03-24
Release date:1995-07-10
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme.
J.Mol.Biol., 250, 1995
176L
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BU of 176l by Molmil
PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME
Descriptor: CHLORIDE ION, T4 LYSOZYME
Authors:Zhang, X.-J, Weaver, L, Dubose, R, Matthews, B.W.
Deposit date:1995-03-24
Release date:1995-07-10
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme.
J.Mol.Biol., 250, 1995
180L
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BU of 180l by Molmil
PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME
Descriptor: LYSOZYME
Authors:Kuroki, R, Weaver, L, Zhang, X.-J, Matthews, B.W.
Deposit date:1995-03-24
Release date:1996-04-03
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.75 Å)
Cite:Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme.
J.Mol.Biol., 250, 1995
178L
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BU of 178l by Molmil
Protein flexibility and adaptability seen in 25 crystal forms of T4 LYSOZYME
Descriptor: CHLORIDE ION, T4 LYSOZYME
Authors:Matsumura, M, Weaver, L, Zhang, X.-J, Matthews, B.W.
Deposit date:1995-03-24
Release date:1995-07-10
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.71 Å)
Cite:Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme.
J.Mol.Biol., 250, 1995
1P56
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Duplication-extension of Helix A of T4 lysozyme
Descriptor: PROTEIN (Lysozyme)
Authors:Sagermann, M, Gay, L, Baase, W.A, Matthews, B.W.
Deposit date:2003-04-25
Release date:2004-05-04
Last modified:2023-08-16
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Relocation or duplication of the helix A sequence of T4 lysozyme causes only modest changes in structure but can increase or decrease the rate of folding.
Biochemistry, 43, 2004
1QSQ
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BU of 1qsq by Molmil
CAVITY CREATING MUTATION
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Lindstrom, J, Matthews, B.W.
Deposit date:1999-06-22
Release date:1999-06-29
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.
Biochemistry, 38, 1999
1NHB
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BU of 1nhb by Molmil
Specificity of ligand binding in a buried non-polar cavity of t4 lysozyme: linkage of dynamics and structural plasticity
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, PHENYLETHANE, ...
Authors:Morton, A, Matthews, B.W.
Deposit date:1995-02-24
Release date:1995-07-10
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: linkage of dynamics and structural plasticity.
Biochemistry, 34, 1995
1P5C
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BU of 1p5c by Molmil
Circular permutation of Helix A in T4 lysozyme
Descriptor: Lysozyme
Authors:Sagermann, M, Gay, L, Baase, W.A, Matthews, B.W.
Deposit date:2003-04-25
Release date:2004-05-04
Last modified:2023-08-16
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:Relocation or duplication of the helix A sequence of T4 lysozyme causes only modest changes in structure but can increase or decrease the rate of folding.
Biochemistry, 43, 2004
1G1W
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BU of 1g1w by Molmil
T4 LYSOZYME MUTANT C54T/C97A/Q105M
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME
Authors:Quillin, M.L, Matthews, B.W.
Deposit date:2000-10-13
Release date:2001-05-09
Last modified:2023-08-09
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme.
Protein Sci., 10, 2001

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