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Asparagine-linked <i>N</i>-glycans on proteins have diverse structures, and their functions vary according to their structures. In recent years, it has become possible to obtain high quantities of <i>N</i>-glycans via isolation and chemical/enzymatic/chemoenzymatic synthesis. This has allowed for progress in the elucidation of <i>N</i>-glycan functions at the molecular level. Interaction analyses with lectins by glycan arrays or nuclear magnetic resonance (NMR) using various <i>N</i>-glycans have revealed the molecular basis for the recognition of complex structures of <i>N</i>-glycans. Preparation of proteins modified with homogeneous <i>N</i>-glycans revealed the influence of <i>N</i>-glycan modifications on protein functions. Furthermore, <i>N</i>-glycans have potential applications in drug development. This review discusses recent advances in the chemical biology of <i>N</i>-glycans.