Faustinus K. Yeboah
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Faustinus K. Yeboah has a total of 5 co-authors. Here are the top co-authors by number of shared publications:
Enrico O. Purisima
Biotechnology Research Institute, 6100 Royalmount Avenue, Montreal, Quebec, Canada H4P-2R2, and Department of Food Science and Agricultural Chemistry, Macdonald Campus, McGill University, 21,111 Lakeshore Road, Ste. Anne de Bellevue, Quebec, Canada H9X 3V9
1 shared publicationInteaz Alli
Biotechnology Research Institute, 6100 Royalmount Avenue, Montreal, Quebec, Canada H4P-2R2, and Department of Food Science and Agricultural Chemistry, Macdonald Campus, McGill University, 21,111 Lakeshore Road, Ste. Anne de Bellevue, Quebec, Canada H9X 3V9
1 shared publicationKonishi Yasuo
Biotechnology Research Institute, 6100 Royalmount Avenue, Montreal, Quebec, Canada H4P-2R2, and Department of Food Science and Agricultural Chemistry, Macdonald Campus, McGill University, 21,111 Lakeshore Road, Ste. Anne de Bellevue, Quebec, Canada H9X 3V9
1 shared publicationShafinaz F. Chowdhury
Biotechnology Research Institute, 6100 Royalmount Avenue, Montreal, Quebec, Canada H4P-2R2, and Department of Food Science and Agricultural Chemistry, Macdonald Campus, McGill University, 21,111 Lakeshore Road, Ste. Anne de Bellevue, Quebec, Canada H9X 3V9
1 shared publicationVaroujan A. Yaylayan
Biotechnology Research Institute, 6100 Royalmount Avenue, Montreal, Quebec, Canada H4P-2R2, and Department of Food Science and Agricultural Chemistry, Macdonald Campus, McGill University, 21,111 Lakeshore Road, Ste. Anne de Bellevue, Quebec, Canada H9X 3V9
1 shared publication
Latest Publications
- 1 January 2004
- Published by American Chemical Society (ACS) in Bioconjugate Chemistry
- Vol. 15 (1) , 27-34
Effect of Limited Solid-State Glycation on the Conformation of Lysozyme by ESI-MSMS Peptide Mapping and Molecular Modeling
Although protein glycation has been implicated in the alteration of protein functionality, both in vivo (in biological systems) and in vitro (in food systems), the effect of the protein-bound glycan moiety on the structure/conformation of proteins that result in the modification of functionality is not clear. In this article, we report a study of the conformational changes of glycated lysozyme using LC-ESI-MSMS peptide mapping, and molecular modeling. A comparison of the RP-HPLC of the tryptic digests of unglycated and glycated lysozyme showed markedly different chromatographic profiles. Analysis of the peptide composition of the chromatographic fractions of the tryptic digests revealed that glycation of lysozyme resulted in the modification of its conformation. Glycation-induced changes in the conformation of lysozyme resulted in the exposure of its active site region to increased proteolytic activity of trypsin. Molecular simulation of triglycated lysozyme also showed that limited glycation of lysozyme caused reorientation of the active site residues (Arg 45, Arg 68, Asn 44, and Trp 62) and increased solvent accessibility into the active site region of the protein. The results of the modeling experiment corroborated the results of the RP-HPLC and ESI-MSMS peptide mapping.
- 1 January 2004
- Published by American Chemical Society (ACS) in Bioconjugate Chemistry
- Vol. 15 (1) , 27-34
Effect of Limited Solid-State Glycation on the Conformation of Lysozyme by ESI-MSMS Peptide Mapping and Molecular Modeling
Although protein glycation has been implicated in the alteration of protein functionality, both in vivo (in biological systems) and in vitro (in food systems), the effect of the protein-bound glycan moiety on the structure/conformation of proteins that result in the modification of functionality is not clear. In this article, we report a study of the conformational changes of glycated lysozyme using LC-ESI-MSMS peptide mapping, and molecular modeling. A comparison of the RP-HPLC of the tryptic digests of unglycated and glycated lysozyme showed markedly different chromatographic profiles. Analysis of the peptide composition of the chromatographic fractions of the tryptic digests revealed that glycation of lysozyme resulted in the modification of its conformation. Glycation-induced changes in the conformation of lysozyme resulted in the exposure of its active site region to increased proteolytic activity of trypsin. Molecular simulation of triglycated lysozyme also showed that limited glycation of lysozyme caused reorientation of the active site residues (Arg 45, Arg 68, Asn 44, and Trp 62) and increased solvent accessibility into the active site region of the protein. The results of the modeling experiment corroborated the results of the RP-HPLC and ESI-MSMS peptide mapping.