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1L21
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BU of 1l21 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 (1.85 Å)
Cite:Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme.
J.Mol.Biol., 210, 1989
1L28
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BU of 1l28 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 (1.9 Å)
Cite:Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.
Science, 239, 1988
1L33
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BU of 1l33 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
1L17
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BU of 1l17 by Molmil
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
1L25
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BU of 1l25 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
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
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
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
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
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
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
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
1KW5
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BU of 1kw5 by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
Deposit date:2002-01-28
Release date:2003-06-03
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.75 Å)
Cite:Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
1LNA
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BU of 1lna by Molmil
A STRUCTURAL ANALYSIS OF METAL SUBSTITUTIONS IN THERMOLYSIN
Descriptor: CALCIUM ION, COBALT (II) ION, DIMETHYL SULFOXIDE, ...
Authors:Holland, D.R, Hausrath, A.C, Juers, D, Matthews, B.W.
Deposit date:1994-05-13
Release date:1995-05-08
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Structural analysis of zinc substitutions in the active site of thermolysin.
Protein Sci., 4, 1995
1LNC
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BU of 1lnc by Molmil
A STRUCTURAL ANALYSIS OF METAL SUBSTITUTIONS IN THERMOLYSIN
Descriptor: CALCIUM ION, DIMETHYL SULFOXIDE, LYSINE, ...
Authors:Holland, D.R, Hausrath, A.C, Juers, D, Matthews, B.W.
Deposit date:1994-05-13
Release date:1995-05-08
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structural analysis of zinc substitutions in the active site of thermolysin.
Protein Sci., 4, 1995
1L12
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BU of 1l12 by Molmil
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
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BU of 1l16 by Molmil
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
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BU of 1l03 by Molmil
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
1L0J
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BU of 1l0j by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
Deposit date:2002-02-11
Release date:2003-06-03
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.98 Å)
Cite:Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
1LNE
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BU of 1lne by Molmil
A STRUCTURAL ANALYSIS OF METAL SUBSTITUTIONS IN THERMOLYSIN
Descriptor: CADMIUM ION, CALCIUM ION, DIMETHYL SULFOXIDE, ...
Authors:Holland, D.R, Hausrath, A.C, Juers, D, Matthews, B.W.
Deposit date:1994-05-13
Release date:1995-05-08
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Structural analysis of zinc substitutions in the active site of thermolysin.
Protein Sci., 4, 1995
1L06
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BU of 1l06 by Molmil
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
1L10
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BU of 1l10 by Molmil
STRUCTURAL STUDIES OF MUTANTS OF THE LYSOZYME OF BACTERIOPHAGE T4. THE TEMPERATURE-SENSITIVE MUTANT PROTEIN THR157 (RIGHT ARROW) ILE
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:Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157----Ile.
J.Mol.Biol., 197, 1987
1L15
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BU of 1l15 by Molmil
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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