How to study proteins by circular dichroism.

By S. Kelly, Thomas J. Jess, N. C. Price. Biochimica et Biophysica Acta, 2005

3,291 citations recorded by the source corpus.

Subfields: Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/4512e2c5aa804a1d77cf5eb5d9de697637ac6b9f

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In Molecular Biology

1. Daniel H. A. Correcirc
2. C. Ramos
3. P. Gill
4. Bijan Ranjbar

In Spectroscopy

1. Daniel H. A. Correcirc
2. C. Ramos
3. P. Gill
4. Bijan Ranjbar

Citations in the corpus

• Circular Dichroism Techniques: Biomolecular and Nanostructural Analyses‐ A Review (2009, background): “Technically, far-UV CD spectra require 20–200 lL of solution containing 1 mg ⁄ mL to 50 lg ⁄ mL protein, in any buffer which does not have a high absorbance in this region of the spectrum (such as high concentrations of dithiothreitol, histidine, or imidazole, for example, cannot be used in the far-”
• The use of circular dichroism spectroscopy to study protein folding, form and function (2009, methodology): “Further information can be found elsewhere (Greenfield, 2006; Kelly et al., 2005).”