CHARMM36m: an improved force field for folded and intrinsically disordered proteins

Keywords

Intrinsically disordered proteinsForce field (fiction)Molecular dynamicsChemistryBiophysicsComputational biologyComputer scienceBiologyComputational chemistryArtificial intelligence

Affiliated Institutions

Related Publications

Optimized Molecular Dynamics Force Fields Applied to the Helix−Coil Transition of Polypeptides

Robert B. Best , Gerhard Hummer

Obtaining the correct balance of secondary structure propensities is a central priority in protein force-field development. Given that current force fields differ significantly ...

2009 The Journal of Physical Chemistry B 879 citations

Balanced Protein–Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein Association

Robert B. Best , Wenwei Zheng , Jeetain Mittal

Some frequently encountered deficiencies in all-atom molecular simulations, such as nonspecific protein-protein interactions being too strong, and unfolded or disordered states ...

2014 Journal of Chemical Theory and Comput... 683 citations

Improved Treatment of the Protein Backbone in Empirical Force Fields

Alexander D. MacKerell , Michael Feig , Charles L. Brooks

Empirical force field-based calculations of proteins, including protein-folding studies, have improved our understanding of the relationship of their structure to their biologic...

2003 Journal of the American Chemical Society 991 citations

AI-based structure prediction empowers integrative structural analysis of human nuclear pores

Shyamal Mosalaganti , Agnieszka Obarska-Kosińska , Marc Siggel +11 more

INTRODUCTION The eukaryotic nucleus protects the genome and is enclosed by the two membranes of the nuclear envelope. Nuclear pore complexes (NPCs) perforate the nuclear envelo...

2022 Science 301 citations

Comparison of multiple Amber force fields and development of improved protein backbone parameters

Viktor Horn̆ák , Robert Abel , Asim Okur +3 more

Abstract The ff94 force field that is commonly associated with the Amber simulation package is one of the most widely used parameter sets for biomolecular simulation. After a de...

2006 Proteins Structure Function and Bioin... 6904 citations

Publication Info

Year: 2016
Type: article
Volume: 14
Issue: 1
Pages: 71-73
Citations: 6736
Access: Closed

External Links

View on DOI.org

Social Impact

Altmetric

CHARMM36m: an improved force field for folded and intrinsically disordered proteins

PlumX Metrics

Social media, news, blog, policy document mentions

Citation Metrics

6736

OpenAlex

Cite This

APA Style

                            
                                
                                    Jing Huang, 
                                
                                    Sarah Rauscher, 
                                
                                    Grzegorz Nawrocki
                                
                                et al.
                            
                            (2016). 
                            CHARMM36m: an improved force field for folded and intrinsically disordered proteins. 
                            Nature Methods
                            , 14
                            (1)
                            , 71-73.
                            https://doi.org/10.1038/nmeth.4067
                        

Identifiers

DOI: 10.1038/nmeth.4067