Development and current status of the CHARMM force field for nucleic acids

By Alexander D. MacKerell, N. Banavali, Nicolas Foloppe. Biopolymers, 2000

975 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/b0b4f1b20a8b0656c0ab187f8638e8445c8edd82

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. Ahmad N. Shuid
2. Robert Kempster
3. Liam J. McGuffin
4. Daniel B. Roche
5. Ali Hassan Ahmed Maghrabi
6. Torsten Schwede
7. Maria T. Buenavista
8. Stuart J. Tetchner

In Molecular Biology

1. Ahmad N. Shuid
2. Robert Kempster
3. Liam J. McGuffin
4. Daniel B. Roche
5. Lukasz Kurgan
6. Ali Hassan Ahmed Maghrabi
7. Vladimir N Uversky
8. Torsten Schwede

Citations in the corpus

• ReFOLD: a server for the refinement of 3D protein models guided by accurate quality estimates (2017, methodology): “The CHARMM22/27 (21) force field (for protein systems, the two are equivalent) was used as the parameter file with default TIP3P water model (22).”
• ROSETTALIGAND: Protein–small molecule docking with full side‐chain flexibility (2006, neutral): “43 The partial charges inside the ligand were linearly scaled to reproduce the total charge of the small molecule.”