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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
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
2LZM
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BU of 2lzm by Molmil
STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME REFINED AT 1.7 ANGSTROMS RESOLUTION
Descriptor: T4 LYSOZYME
Authors:Weaver, L.H, Matthews, B.W.
Deposit date:1986-08-18
Release date:1986-10-24
Last modified:2024-05-22
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution.
J.Mol.Biol., 193, 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
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