ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES

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本数据集主题为通过与α螺旋（alpha-helix）偶极相互作用的设计突变增强蛋白质热稳定性。数据集标识：T4溶菌酶（T4 LYSOZYME）；作者：Nicholson, H、Matthews, B.W.；提交日期：1989年5月1日；发布日期：1990年1月15日；最后修改日期：2024年5月22日；研究方法：X射线衍射（X-RAY DIFFRACTION，分辨率1.85埃（Å）；引用文献：Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles. *Nature*, 336, 1988。