The molecular basis for the chemical denaturation of proteins by urea

By B. Bennion, V. Daggett. Proceedings of the National Academy of Sciences of the United States of America, 2003

840 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/069eadd03c8f643ba6980e1d1c87c6cf3f9983c6

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. Yaakov Levy
2. José N. Onuchic
3. W. Eaton

In Molecular Biology

1. Yaakov Levy
2. Benjamin Schuler
3. W. Eaton
4. José N. Onuchic
5. Martin Weigt

In Spectroscopy

1. José N. Onuchic
2. Yaakov Levy

Citations in the corpus

• Water mediation in protein folding and molecular recognition. (2006, background): “Several lines of evidence exist for an indirect unfolding mechanism in which urea perturbs the water structure and dynamics by weakening the hydrogen bond network of the water and thus disorders the water structure so that hydrophobic molecules are more easily solvated (10, 55).”
• Protein folding studied by single-molecule FRET. (2008, background): “The discrepancy between the ensemble SAXS and singlemolecule FRET result is yet to be explained [31 ], particularly as continuous expansion of protein L is observed upon the addition of urea in molecular dynamics simulations in explicit water [31 ,51].”