2007 - Benjamin Franklin Medal, Franklin Institute
1994 - Oesper Award, University of Cincinnati and American Chemical Society
1993 - Member of the National Academy of Sciences
1983 - Fellow of John Simon Guggenheim Memorial Foundation
1980 - Fellow of the American Association for the Advancement of Science (AAAS)
His primary areas of study are Biochemistry, Mass spectrometry, Peptide sequence, Protein primary structure and Chromatography. In Biochemistry, he works on issues like Angiogenesis, which are connected to Endothelium, Growth inhibition, Cell growth, In vitro and Methionine. His study on Mass spectrometry is covered under Analytical chemistry.
His research integrates issues of Lipocalin, Glycosylation, In situ hybridization and Glycoprotein in his study of Peptide sequence. His Protein primary structure research incorporates elements of Aminoacyl tRNA synthetase, Tandem mass spectrometry, Edman degradation, Oligonucleotide and Streptomyces. His studies deal with areas such as Oligopeptide, Peptide, Molecular mass and Chemical ionization as well as Chromatography.
The scientist’s investigation covers issues in Mass spectrometry, Chromatography, Biochemistry, Analytical chemistry and Peptide sequence. His study in Mass spectrometry is interdisciplinary in nature, drawing from both Ionization and Molecular mass. Klaus Biemann focuses mostly in the field of Chromatography, narrowing it down to topics relating to Peptide and, in certain cases, Dissociation and Stereochemistry.
His Biochemistry study frequently draws connections between related disciplines such as Molecular biology. His Analytical chemistry study incorporates themes from Ion and Protonation. His Edman degradation and Protein sequencing study in the realm of Peptide sequence connects with subjects such as Bacteriorhodopsin.
Klaus Biemann mainly focuses on Biochemistry, Mass spectrometry, Chromatography, Peptide and Analytical chemistry. His work is connected to Amino acid, Enzyme, Peptide sequence, Protein primary structure and Sequence, as a part of Biochemistry. His Mass spectrometry research is multidisciplinary, incorporating elements of Ionization, Matrix-assisted laser desorption/ionization and Matrix isolation.
Specifically, his work in Chromatography is concerned with the study of Protein mass spectrometry. His Peptide research is multidisciplinary, relying on both Electrospray ionization, Adduct, Organic chemistry, Dissociation and Stereochemistry. His Analytical chemistry research integrates issues from Ion, Protonation and Crystallography.
His primary areas of investigation include Biochemistry, Sulfation, Peptide, Enzyme and Amino acid. His research in the fields of Binding site, Glycosaminoglycan, In vitro and METAP2 overlaps with other disciplines such as Heparin lyase. He interconnects Oligosaccharide, Molecular mass and Chromatography in the investigation of issues within Sulfation.
His work carried out in the field of Peptide brings together such families of science as Chelation, Organic chemistry and Mass spectrometry. His Mass spectrometry research is within the category of Analytical chemistry. His study in Amino acid is interdisciplinary in nature, drawing from both Myoglobin, Sperm whale and Electrospray ionization.
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Contributions of mass spectrometry to peptide and protein structure.
Klaus Biemann.
Journal of Mass Spectrometry (1988)
Mass spectrometric determination of the amino acid sequence of peptides and proteins
Klaus Biemann;Stephen A. Martin.
Mass Spectrometry Reviews (1987)
The composition of the atmosphere at the surface of Mars
Tobias Owen;K. Biemann;D. R. Rushneck;J. E. Biller.
Journal of Geophysical Research (1977)
The search for organic substances and inorganic volatile compounds in the surface of Mars
K. Biemann;J. Oro;P. Toulmin;L. E. Orgel.
Journal of Geophysical Research (1977)
Collision-induced fragmentation of (M + H)+ ions of peptides. Side chain specific sequence ions
Richard S. Johnson;Stephen A. Martin;Klaus Biemann.
International Journal of Mass Spectrometry and Ion Processes (1988)
Novel fragmentation process of peptides by collision-induced decomposition in a tandem mass spectrometer: differentiation of leucine and isoleucine.
Johnson Rs;Martin Sa;Biemann K;Stults Jt.
Analytical Chemistry (1987)
Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin
Eric C. Griffith;Zhuang Su;Benjamin E. Turk;Shaoping Chen.
Chemistry & Biology (1997)
Characterization by tandem mass spectrometry of structural modifications in proteins
Klaus Biemann;Hubert A. Scoble;Hubert A. Scoble.
Science (1987)
n-Tetradecanoyl is the NH2-terminal blocking group of the catalytic subunit of cyclic AMP-dependent protein kinase from bovine cardiac muscle.
Steven A. Carr;K. Biemann;Shozo Shoji;David C. Parmelee.
Proceedings of the National Academy of Sciences of the United States of America (1982)
Amino acid sequence of bacteriorhodopsin
H G Khorana;G E Gerber;W C Herlihy;C P Gray.
Proceedings of the National Academy of Sciences of the United States of America (1979)
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