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PDB: 6 件
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
分子名称: T4 LYSOZYME
著者Daopin, S, Matthews, B.W.
登録日1991-01-28
公開日1991-10-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.8 Å)
主引用文献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
1L47
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BU of 1l47 by Molmil
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
分子名称: T4 LYSOZYME
著者Daopin, S, Matthews, B.W.
登録日1991-01-28
公開日1991-10-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献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
1L45
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BU of 1l45 by Molmil
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
分子名称: T4 LYSOZYME
著者Daopin, S, Matthews, B.W.
登録日1991-01-28
公開日1991-10-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献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
1L46
DownloadVisualize
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
分子名称: T4 LYSOZYME
著者Daopin, S, Matthews, B.W.
登録日1991-01-28
公開日1991-10-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献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
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
分子名称: T4 LYSOZYME
著者Daopin, S, Matthews, B.W.
登録日1991-01-28
公開日1991-10-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.8 Å)
主引用文献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
1L44
DownloadVisualize
BU of 1l44 by Molmil
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
分子名称: T4 LYSOZYME
著者Daopin, S, Matthews, B.W.
登録日1991-01-28
公開日1991-10-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献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

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