  We present a review of a series of contact maps for the determination of
native interactions in proteins and nucleic acids based on a
distance-threshold. Such contact maps are mostly based on physical and chemical
construction, and yet they are sensitive to some parameters (e.g. distances or
atomic radii) and can neglect some key interactions. Furthermore, we also
comment on a new class of contact maps that only requires geometric arguments.
The contact map is a necessary ingredient to build a robust G\=oMartini model
for proteins and their complexes in the Martini 3 force field. We present the
extension of a popular structure-based G\=o-like approach for the study of
protein-sugar complexes, and also limitations of this approach are discussed.
The G\=oMartini approach was first introduced by Poma et al. J. Chem. Theory
Comput. 2017, 13(3), 1366-1374 in Martini 2 force field and recently, it has
gained the status of gold-standard for protein simulation undergoing
conformational changes in Martini 3 force field. We discuss several studies
that have provided support to this approach in the context of the biophysical
community.
