Glycans attached to proteins and lipids exert their biological functions through dynamic intra- and intermolecular interactions. Owing to their intrinsic flexibility, however, glycan conformations are often only partially resolved by X-ray crystallography or cryo-electron microscopy, leaving important structural details unclear. Nuclear magnetic resonance (NMR) spectroscopy and molecular dynamics (MD) simulations provide complementary approaches for characterizing the conformational ensembles and dynamic behavior of glycans in solution. Integration of experimental and computational methods enables quantitative evaluation of conformer populations and facilitates interpretation of glycan recognition by lectins, antibodies, and enzymes. Advances in this area are expected to enhance our understanding of glycan-mediated biological processes and support applications in drug discovery and glycoengineering. Continued efforts to improve quantitative prediction of glycan conformations will be essential for advancing structural glycobiology.