Considering the small number of papers assessing the conformational profile of glycoproteins through molecular dynamics (MD) simulations, the current work reports on a systematic analysis of the performance of the GROMOS96 43a1 force field and Löwdin HF/6-31G( * *)-derived atomic charges in the conformational description of glycoproteins. The results substantiate the accuracy of the computational representation of glycoprotein conformational ensembles in aqueous solution based on their agreement to available experimental information, supporting further contributions of computational techniques, mainly MD, in future studies on the characterization of glycoprotein structure and function.