Estimation of the number of α‐helical and β‐strand segments in proteins using circular dichroism spectroscopy

By Narasimha Sreerama, S. Venyaminov, Robert W. Woody. Protein Science, 2008

631 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/4e8f20a2b10e153d9f88347e329e61ee56152af8

How researchers see this paper

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

In Materials Chemistry

1. B. Wallace
2. Lee Whitmore
3. Robert W. Woody
4. Narasimha Sreerama
5. N. C. Price
6. Thomas J. Jess
7. S. Kelly

In Molecular Biology

1. B. Wallace
2. Lee Whitmore
3. Robert W. Woody
4. Narasimha Sreerama
5. Thomas J. Jess
6. N. C. Price
7. S. Kelly

In Spectroscopy

1. B. Wallace
2. Lee Whitmore

Citations in the corpus

• DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data (2004, methodology): “For example, if the unknown protein contains a significant amount of polyproline II structure, it may be better analysed with the databases that contain this component ( 4 ,16).”
• Structural composition of βI‐ and βII‐proteins (2003, background): “The CD spectra of carbonic anhydrase and chymotrypsinogen are taken from Pancoska et al. (1995), and those of rat intestinal fatty-acid binding protein and green fluorescent protein are from Sreerama et al. (1999).”