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Urea denaturation, unfolded proteins circular dichroism

For example, increasing the temperature or addition of chemical denaturants such as urea or guanidinium hydrochloride (GuHCl) produce changes in fluorescence or circular dichroism spectra of proteins in solution consistent with unfolding of the protein structure (Figures 5.10 and 5.11). [Pg.110]

Most physical properties of a protein change substantially when it unfolds. Consequently, many techniques can be used to follow unfolding those used most often are ultraviolet difference spectroscopy, circular dichroism, optical rotation, fluorescence, and NMR spectroscopies. One of the most popular methods of estimating protein stability is based on monitoring urea and guanidine hydrochloride denaturation curves of the protein. ... [Pg.286]

See other pages where Urea denaturation, unfolded proteins circular dichroism is mentioned: [Pg.273]    [Pg.24]    [Pg.224]    [Pg.6]    [Pg.330]    [Pg.241]    [Pg.144]    [Pg.6833]    [Pg.377]   
See also in sourсe #XX -- [ Pg.201 , Pg.203 , Pg.205 , Pg.206 ]



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Circular dichroism protein unfolding

Circular proteins

Denaturation unfolded proteins

Protein circularization

Protein denaturants

Protein unfolding

Proteins denaturation

Proteins denaturing

Unfolded

Unfolded proteins

Unfolders

Unfolding denaturing

Urea denaturation, unfolded proteins

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