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Peter Roepstorff

Peter Roepstorff, Dr. h.c. (born June 10, 1942) is a pioneering Danish scientist recognised for his significant contributions to protein structure/function analysis by mass spectrometry. His work laid the foundation for modern proteomics, particularly in studies of post-translational modifications.

Early Life and Education

Peter Roepstorff was born in Copenhagen, Denmark, in 1942. He received his Diplôme d'études supérieures in physiological chemistry from the Université d'Aix-Marseille in 1965, followed by a degree in Chemical Engineering from the Danish Technical University in 1966. His early interest in protein chemistry led him to pursue research in the emerging field of mass spectrometry.

Academic Career and Research

Peter Roepstorff began his academic career as a Research Associate at the Danish Institute of Protein Chemistry in 1966. In 1974, he joined the University of Southern Denmark in Odense (then Odense University) as an associate professor in the newly established Department of Molecular Biology. He became a full professor in 1995.

Roepstorff's early publications were transformative in demonstrating the potential of mass spectrometry for studying peptide and protein modifications. One of his significant contributions was the application of mass spectrometry to studying vitamin K-dependent gamma-carboxylation in prothrombin, a key protein in blood clotting. His 1974 and 1975 publications (PMID: 4528109, PMID: 50323) demonstrated how mass spectrometry could detect and characterise protein modifications critical for biological function. This work opened new avenues for studying post-translational modifications, marking an important step in bridging analytical chemistry and biomedical research. Roepstorff's early efforts helped lay the foundation for the subsequent revolution in proteomics.

Roepstorff is renowned for his pioneering contributions to protein mass spectrometry, including the Roepstorff-Fohlman nomenclature (PMID: 6525415) for peptide fragmentation in 1984. This nomenclature standardised the naming of fragment ions generated during peptide dissociation in mass spectrometry, specifically the a, b, and y ions, which are now widely used in mass spectrometry-based proteomics. The nomenclature remains a cornerstone in the field, facilitating peptide sequencing and the identification of post-translational modifications.

His seminal work (PMID: 8329463) introduced the concept of mass spectrometric molecular weight information for protein identification using sequence databases. Building on earlier work on peptide charting by mass spectrometry (PMID 2762311) this 1993 paper introduced the concept of using mass spectrometric molecular weight information to identify proteins by matching experimentally determined peptide mass maps to amino acid sequences in protein databases. Such peptide mass fingerprinting, revolutionised the field by dramatically increasing the speed and accuracy of protein identification, thereby giving birth to the field of proteomics.

In 1999, Peter Roepstorff supervised the development of a highly sensitive method for preparing and purifying complex peptide mixtures using nanoliter-scale reversed-phase columns, as detailed in the paper "Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry" (PMID: 10093212). This technique enabled the efficient separation and purification of peptides before mass spectrometry analysis, thereby improving the sensitivity and accuracy of peptide analysis. The method was particularly effective for analysing complex biological samples, leading to enhanced mass spectrometry data quality, which is critical for accurate protein identification. This breakthrough in sample preparation became a cornerstone in proteomics and laid the foundation for tip-based peptide cleaning. It remains widely used in modern proteomics protocols.

Peter Roepstorff contributed to phosphoproteomics during the early 2000’s (PMID: 11680869), i.e. large-scale analysis of phosphorylated proteins.  Roepstorff's vision for using affinity-enrichment and mass spectrometry to study post-translational modifications by “modification-specific proteomics” is convincingly illustrated in the 2005 paper, "Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns" (PMID: 15858219). Selective enrichment of phosphorylated peptides is a cornerstone in current phosphoproteomics research.

Peter Roepstorff founded the Protein Research Group at the University of Southern Denmark, a globally recognised centre for mass spectrometry, protein science, and proteomics.

Awards and Honours

Throughout his career, Roepstorff received numerous accolades, including the Villum Kann Rasmussen Prize (1989), Kaj Linderstrøm-Lang Gold Medal (2002), Novo Nordisk Award (2004), and HUPO Distinguished Achievement Award in Proteomic Sciences (2007). He was awarded the Thomson Medal in 2009 for his contributions to mass spectrometry. Roepstorff holds honorary doctorates from Uppsala University, Sweden and the Danish Technical University.

Legacy

Roepstorff's contributions have been widely cited, with more than 25,000 citations to his works and an h-index of 74. His influence continues to shape the fields of proteomics, mass spectrometry, and post-translational modification analysis. Link to publications.

Participation in the Galathea 3 Expedition

Peter Roepstorff participated in the Galathea 3 expedition, and his project aimed to identify and characterise fluorescent proteins from marine organisms.

External Links

Last Updated 20.10.2024