Single-Molecule Force Microscopy of Circularly Permuted Green Fluorescent Protein
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概要
- 論文の詳細を見る
We introduced new termini on surface loops of green fluorescent protein (GFP) by linking the original ones. The mechanical properties of two circularly permuted GFPs (cpGFPs) were examined by atomic force microscopy (AFM) and compared with those of the base GFPs. The unfolding results revealed different levels of the reduced mechanical stability of cpGFPs, and these levels were related to the proximity of the newly introduced termini to the central ‘$\beta$-can’.
- 2004-08-15
著者
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Kogure Takako
Laboratory For Cell Function Dynamics Advanced Technology Development Center Brain Science Institute
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Miyawaki Atsushi
Laboratory For Cell Function And Dynamics Advanced Technology Development Center Brain Science Insti
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Hara Masahiko
Local Spatio-temporal Function Frontier Research System The Institute Of Physical And Chemical Resar
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Nakajima Ken
Local Spatio-temporal Functions Laboratory Frontier Research System Riken (the Institute Of Physical
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Miyawaki Atsushi
Laboratory for Cell Function Dynamics, Advanced Technology Development Center, Brain Science Institute, RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan
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Wang Tong
Local Spatio-Temporal Functions Laboratory, Frontier Research System, RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan
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Yokokawa Shinobu
Local Spatio-Temporal Functions Laboratory, Frontier Research System, RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan
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