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1L31
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BU of 1l31 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 (1.8 Å)
Cite:Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.
Science, 239, 1988
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:2024-10-30
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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BU of 1l49 by Molmil
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
1L19
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BU of 1l19 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 (1.7 Å)
Cite:Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles.
Nature, 336, 1988
1L22
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BU of 1l22 by Molmil
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:2024-05-22
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
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
1L61
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BU of 1l61 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, 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
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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
1L27
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BU of 1l27 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 (1.8 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
1L39
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BU of 1l39 by Molmil
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:2024-05-22
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
1L62
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BU of 1l62 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, 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 (1.7 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
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
1L73
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BU of 1l73 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:2020-07-22
Method:X-RAY DIFFRACTION (2.05 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
1L65
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BU of 1l65 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
1L57
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BU of 1l57 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, CHLORIDE ION, 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 (1.9 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
1L72
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BU of 1l72 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:2017-11-29
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
1L46
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BU of 1l46 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
1L42
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BU of 1l42 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
1L59
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BU of 1l59 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, 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
1L70
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BU of 1l70 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:2017-11-29
Method:X-RAY DIFFRACTION (1.9 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

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