Harnessing the unique structural properties of isolated α-helices.

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作者： Carter J,Swanson ^[1] ; Sivaraj,Sivaramakrishnan ^[2]

作者单位： From the Departments of Biophysics. ^[1] From the Departments of Biophysics, Cell and Developmental Biology, and Biomedical Engineering, University of Michigan, Ann Arbor, Michigan 48109 sivaraj@umich.edu. ^[2]

关键词 Biosensor Coiled-coil ER/K Alpha-Helix ER/K Linker Fluorescence Resonance Energy Transfer (FRET)Myosin Protein Structure Protein-Protein Interaction Single Alpha-helical Domain (SAH)

主题词氨基酸特征结构(Amino Acid Motifs);精氨酸(Arginine);C肽(C-Peptide);圆二色性(Circular Dichroism);人类(Humans);赖氨酸(Lysine);蛋白质相互作用域和基序(Protein Interaction Domains and Motifs);蛋白质结构, 二级(Protein Structure, Secondary);蛋白质结构, 三级(Protein Structure, Tertiary);核糖核酸酶, 胰腺(Ribonuclease, Pancreatic);构效关系(Structure-Activity Relationship)

DOI 10.1074/jbc.R114.583906

PMID 25059657

发布时间 2021-10-21

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The Journal of biological chemistry

2014年289卷37期

25460-7页

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Harnessing the unique structural properties of isolated α-helices.

The Journal of biological chemistry

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Harnessing the unique structural properties of isolated α-helices.

The Journal of biological chemistry

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The Journal of biological chemistry

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