**4. Conclusion**

Due to the inherent complexity of protein glycosylation, better reagents and workflows are required in order to thoroughly and accurately characterize the glycosylation profile within a sample of interest. Intact glycopeptide identification (glycosite and glycan composition) has emerged as a more effective means to study heterogeneity, to investigate disease biomarkers and to characterize therapeutic proteins. Fortunately, several notable advances have arisen in the last few years. These advances include chemical enrichment strategies, engineered lectins with improved specificity, a greater selection of site-specific proteases, more sophisticated mass spectrometry methods/instruments and finally the development of computer algorithms designed for deconvolution of glycopeptide fragmentation spectra. Although challenges remain, these advances have certainly simplified the study of protein glycosylation.

## **Acknowledgements**

The authors acknowledge New England Biolabs, James V. Ellard and Donald G. Comb for research support.

*Improving the Study of Protein Glycosylation with New Tools for Glycopeptide Enrichment DOI: http://dx.doi.org/10.5772/intechopen.97339*
