Random-coil behavior and the dimensions of chemically unfolded proteins.

By J. Kohn, I. Millett, J. Jacob, B. Žagrović, T. Dillon, N. Cingel, Robin S. Dothager, S. Seifert, P. Thiyagarajan, Tobin R. Sosnick and 5 more. Proceedings of the National Academy of Sciences of the United States of America, 2004

663 citations recorded by the source corpus.

Subfields: Cell Biology, Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/fd174f6645c0d46482c972711c3b989f96b6e2b9

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In Materials Chemistry

1. W. Eaton

In Molecular Biology

1. Benjamin Schuler
2. W. Eaton

Citations in the corpus

• Sampling bottlenecks in de novo protein structure prediction (2009, neutral): “18 10 cnl ] [    ( 6 ) where  is the ellipticity measured in millidegrees, c is the molar concentration of”
• Protein folding studied by single-molecule FRET. (2008, background): “These single-molecule FRET studies, together with ensemble SAXS and NMR studies on unfolded proteins [54‐56], suggest that unfolded proteins behave essentially as homopolymers at the highest denaturant concentration, as evidenced in particular by the finding that Rg depends on chain length and is in”