A twist in the road less traveled: The AMBER ff15ipq-m force field for protein mimetics.

ABSTRACT: We present a new force field, AMBER ff15ipq-m, for simulations of protein mimetics in applications from therapeutics to biomaterials. This force field is an expansion of the AMBER ff15ipq force field that was developed for canonical proteins and enables the modeling of four classes of artificial backbone units that are commonly used alongside natural α residues in blended or "heterogeneous" backbones: chirality-reversed D-α-residues, the C_α-methylated α-residue Aib, homologated β-residues (β³) bearing proteinogenic side chains, and two cyclic β residues (β^cyc; APC and ACPC). The ff15ipq-m force field includes 472 unique atomic charges and 148 unique torsion terms. Consistent with the AMBER IPolQ lineage of force fields, the charges were derived using the Im

SUBMITTER: Bogetti AT 

PROVIDER: S-EPMC7419161 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature