The use of circular dichroism in the investigation of protein structure and function.

By S. Kelly, N. C. Price. Current protein and peptide science, 2000

1,130 citations recorded by the source corpus.

Subfields: Atomic and Molecular Physics, and Optics, Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/2edd95c61e875fe7d0138509858f66daed7de06e

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Atomic and Molecular Physics, and Optics

1. W. Sparks
2. James Hough
3. I. Neill Reid
4. Vladimir N Uversky

In Molecular Biology

1. V. Receveur-Bréchot
2. Sonia Longhi
3. Vladimir N Uversky
4. Bruno Canard
5. J. Bourhis
6. P. Gill
7. Bijan Ranjbar
8. A. Keith Dunker

In Spectroscopy

1. V. Receveur-Bréchot
2. P. Gill
3. I. Neill Reid
4. Vladimir N Uversky
5. 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-”
• Circular polarization in scattered light as a possible biomarker (2009, methodology): “Even if local enantiomeric excesses of optically active minerals were to exist, it is expected that they would be distinguishable from biological matter by their spectral properties [1, 5].”
• Assessing protein disorder and induced folding (2005, background): “Disulfide bonds give rise to broad weak signals throughout the near-UV spectrum.(187) The near-UV CD spectrum therefore provides a detailed fingerprint of the tertiary structure around these specific residues.”