Michael Augustine Raftery
Abstract Michael Raftery was an Irish-born scientist who spent most of his career in the USA, where he made substantial and innovative contributions to the understanding of the structure and function of important proteins. Early in his career, he identified effective methods for determining the sequence of amino acids which form the building blocks of all proteins. In parallel, he carried out nuclear magnetic resonance spectroscopy experiments on an enzyme, lysozyme; this natural antibiotic breaks down the walls of bacteria by attacking the sugar–amino acids from which the wall is structured. He also studied the essential oxygen-transporting protein haemoglobin. In the 1970s, his interests turned to the acetylcholine receptor (AChR), the muscle membrane protein that is essential for receiving the chemical signal acetylcholine, required for transmission of impulses from the motor nerve to muscle. He purified the protein, demonstrated that it had four distinct but evolutionarily related subunits and, by obtaining the sequence of amino acids, allowed construction of the first cDNA probes that led to the cloning of the genes for this protein. Similarly, he purified the voltage-gated sodium channel, responsible for the conduction of the nerve impulses, and contributed to the cloning of this essential membrane ion channel. In 1971, Raftery was awarded the Doctor of Science degree from the National University of Ireland in recognition of his outstanding early research contributions, followed by Doctor of Laws in 1987. He was elected to the Royal Society in 1986.
Authors
- Daniel Raftery (ORCID: https://orcid.org/0000-0003-2467-8118)
- Angela Vincent (ORCID: https://orcid.org/0000-0003-2395-8695)
Institutions
- University of Washington (US)
- University of Oxford (GB)
Publication Details
- Journal
- Biographical Memoirs of Fellows of the Royal Society
- Published
- 2025-11-28
- DOI
- https://doi.org/10.1098/rsbm.2025.0005
- Primary Topic
- ATP Synthase and ATPases Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00