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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
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
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
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
1L34
HIGH-RESOLUTION STRUCTURE OF THE TEMPERATURE-SENSITIVE MUTANT OF PHAGE LYSOZYME, ARG 96 (RIGHT ARROW) HIS
Descriptor:
T4 LYSOZYME
Authors:
Weaver, L.H
,
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:
High-resolution structure of the temperature-sensitive mutant of phage lysozyme, Arg 96----His.
Biochemistry, 28, 1989
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
1L32
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
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
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
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
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
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
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
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
1L35
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
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
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PDB entries from 2024-10-16