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nanoDSF is a modified Differential Scanning Fluorimetry method to determine protein stability employing intrinsic tryptophan or tyrosin fluorescence.〔(【引用サイトリンク】title=NanoTemper Technologies GmbH: nanoDSF )〕 nanoDSF was developed by NanoTemper Technologies GmbH, a German high tech company with headquarters in Munich. Protein stability is typically addressed by thermal or chemical unfolding experiments.〔(【引用サイトリンク】title=Thermal denaturation assays in chemical biology. )〕 In thermal unfolding experiments, a linear temperature ramp is applied to unfold proteins, whereas chemical unfolding experiments use chemical denaturants in increasing concentrations. The thermal stability of a protein is typically described by the 'melting temperature' or 'Tm', at which 50% of the protein population is unfolded, corresponding to the midpoint of the transition from folded to unfolded. In contrast to conventional DSF methods, nanoDSF uses tryptophan or tyrosin fluorescence to monitor protein unfolding. Both the fluorescence intensity and the fluorescence maximum strongly depends on the close surroundings of the tryptophan.〔(【引用サイトリンク】title=Principles of Fluorescence Spectroscopy )〕 Therefore, the ratio of the fluorescence intensities at 350 nm and 330 nm is suitable to detect any changes in protein structure, for example due to protein unfolding. Its applications include antibody engineering, membrane protein research, quality control and formulation development.〔(【引用サイトリンク】title=Application Notes: nanoDSF Technology )〕 == References == 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「NanoDSF」の詳細全文を読む スポンサード リンク
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