. Author manuscript; available in PMC: 2015 May 11.

Published in final edited form as: Chem Soc Rev. 2014 Apr 23;43(13):4871–4893. doi: 10.1039/c4cs00048j

Table 1.

Summary of the different systems studied with the CG force field.

Applications	Methodology used	Total Time	References
Αβ_1-40, Αβ_1-42,	HT-REMD	70.0 μs	167
WT(D23N) monomers and dimers		97.5 μs	168
Trimers of Αβ_17-42 and interactions with drugs	REMD	16.4 μs	96
Aggregation of 3- to 20-mers of amyloid fragments	MD ART REMD	30.0 μs no 120.0 μs	149, 150, 152 80,150 23, 68, 99, 149-153
Size of the primary nucleus for fibril formation	MD REMD	33.8 μs 90.0 μs	158 99, 153
Peptide Structure Prediction and Conformations of protein fragments	PEP-FOLD	no	177, 178, 180, 182-189
Protein-peptide interactions	PEP-FOLD	no	190-194
Design of immunogenic and antiviral peptides	PEP-FOLD	no	195-201
Impact of macromolecules and hydrodynamics	MUPHY/OPEP	no	this work
RNA and DNA folding	MD, REMD, ST	85.0 μs	231, 233, this work
Thermophilic and mesophilic proteins	REMD	72.0 μs	this work
Impact of shear flow	MUPHY/OPEP	30 ns	this work
Virtual reality	Interactive MD	0.2 ns	this work