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Updated: Jun 30, 2026

Analyzing and Building Nucleic Acid Structures with 3DNA
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托芬侧链的静电相互作用决定了设计的β-hairpin"trpzip2"中的边对面与平行移位的托芬侧链几何形状

Olgun Guvench1, Charles L Brooks

  • 1Department of Molecular Biology (TPC-6), The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

Journal of the American Chemical Society
|March 31, 2005
PubMed
概括

静电多极时刻对于蛋白质中托侧链相互作用至关重要. 删除这些时刻会改变芳香相互作用的几何结构,影响蛋白质结构预测和对接模型.

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