Klaus Biemann, Professor Emeritus, Massachusetts Institute of Technology (MIT), Cambridge, USA, has passed away on June 2, 2016.
Professor Biemann’s research focused on mass spectrometry. He pioneered its use for the analysis of protein structures. Using this approach, he discovered the sequence of the protein bacteriorhodopsin, among others. Biemann has been called the “father of organic mass spectrometry” and his work has laid the groundwork for proteomics, the study of the structure and function of all proteins produced by an organism.
Klaus Biemann studied chemistry at the University of Innsbruck, Austria, where he received his Ph.D. in organic chemistry in 1951. He remained there as Lecturer until 1955, when he joined MIT to perform postdoctoral research with George H. Büchi. In 1957, Biemann started his first faculty position as Instructor in the analytical chemistry department at MIT. He was appointed as Assistant Professor in 1959, promoted to Associate Professor in 1962, and to Full Professor in 1963. In 1976, Biemann led a team that sent a miniaturized mass spectrometer to Mars as part of NASA’s Viking Mission. He remained at MIT until his retirement.
Among many other honors, Professor Biemann received the Benjamin Franklin Medal in Chemistry in 2007, the Thomson Medal in 1991, the first Field and Franklin Award in Applied Mass Spectrometry from the American Chemical Society (ACS) in 1986, and the Exceptional Scientific Achievement Medal from NASA in 1977.
Selected Publications by Klaus Biemann
- Structure Determination of Natural Products by Mass Spectrometry,
Annu. Rev. Anal. Chem. 2015, 8, 1–19.
- Laying the groundwork for proteomics: Mass spectrometry from 1958 to 1988,
J. Proteomics 2014, 107, 62–70.
- Peptide Compositions of the Cerebrovascular and Senile Plaque Core Amyloid Deposits of Alzheimer′s Disease,
D. L. Miller, I. A. Papayannopoulos, J. Styles, S. A. Bobin, Y. Y. Lin, K. Biemann, K. Iqbal,
Arch. Biochem. Biophys. 1993, 301, 41–52.
- Contributions of mass spectrometry to peptide and protein structure,
Biol. Mass Spectrom. 1988, 16, 99–111.
- Novel fragmentation process of peptides by collision-induced decomposition in a tandem mass spectrometer: differentiation of leucine and isoleucine,
R. S. Johnson, S. A. Martin, K. Biemann, J. T. Stults, J. T. Watson,
Anal. Chem. 1987, 59, 2621–2625.
- Mass spectrometric determination of the amino acid sequence of peptides and proteins,
K. Biemann, S. A. Martin,
Mass Spectrom. Rev. 1987, 6, 1–75.
- n-Tetradecanoyl is the NH2-terminal blocking group of the catalytic subunit of cyclic AMP-dependent protein kinase from bovine cardiac muscle.,
S. A. Carr, K. Biemann, S. Shoji, D. C. Parmelee, K. Titani,
Proc. Natl. Acad. Sci. USA 1982, 79, 6128–6131.
- Amino acid sequence of bacteriorhodopsin.,
H. G. Khorana, G. E. Gerber, W. C. Herlihy, C. P. Gray, R. J. Anderegg, K. Nihei, K. Biemann,
Proc. Natl. Acad. Sci. USA 1979, 76, 5046–5050.