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1L09	CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME Descriptor: T4 LYSOZYME Authors: Dao-Pin, S, Bell, J, 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
1L0J	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
1L0K	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 (2.02 Å) Cite: Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability BIOPHYS.CHEM., 100, 2003
1L10	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
1L11	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
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
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
1L14	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
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
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
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
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
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
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
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: 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
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: 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	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
1L24	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
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
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
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: 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
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
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
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
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

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