Benjamin Schuler
Molecular Biology · 2002–2018
A researcher in the Science corpus: 3 papers; trusts 1 researcher and is trusted by 1 researcher here, as inferred from the citation graph.
Subfields
- Molecular Biology — 25 citations into it; #15,131 of 17,773 by trust here, #9,476 by citations
Whom Benjamin Schuler trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
Who trusts Benjamin Schuler overall
Papers from Benjamin Schuler's perspective
Ordered by how strongly the researchers Benjamin Schuler trusts endorse each paper. Same corpus, a different order for every researcher.
- Microscopic Theory of Protein Folding Rates.II: Local Reaction Coordinates and Chain Dynamics
- Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy (Nature)
- The molecular basis for the chemical denaturation of proteins by urea (Proceedings of the National Academy of Sciences of the United States of America)
- Mechanical processes in biochemistry. (Annual Review of Biochemistry)
- Fluorescence-aided molecule sorting: Analysis of structure and interactions by alternating-laser excitation of single molecules (Proceedings of the National Academy of Sciences of the United States of America)
- The protein folding 'speed limit'. (Current Opinion in Structural Biology)
- Random-coil behavior and the dimensions of chemically unfolded proteins. (Proceedings of the National Academy of Sciences of the United States of America)
- The Helix-Coil Kinetics of a Heteropeptide
- Is there a unifying mechanism for protein folding?
- Ultrafast folding of α3D: A de novo designed three-helix bundle protein (Proceedings of the National Academy of Sciences of the United States of America)
Their papers
- Extreme disorder in an ultra-high-affinity protein complex (2018) — 588 citations
- Protein folding studied by single-molecule FRET. (2008) — 661 citations
- Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy (2002) — 836 citations