Proteins: from Chemical to Physiological Mechanism 26 October 2001

Meeting report report

The Molecular Enzymology Group of the Biochemical Society by David Trentham held a special 1-day meeting at the Royal Society on ‘Proteins: (National Institute of Medical

from Chemical to Physiological Mechanism’.The aim of the Research, Mill Hill) and Downloaded from http://portlandpress.com/biochemist/article-pdf/24/3/31/3597/bio024030031.pdf by guest on 01 October 2021 meeting was to inform and stimulate discussion on kinetic Michael Greeves approaches to the life sciences by bringing together work on (University of Kent) dynamic aspects of protein function.The meeting also honoured Professor H. (Freddie) Gutfreund, FRS, on his 80th birthday. Professor Gutfreund persuaded the Executive Committee of the Society to found the Molecular Enzymology Group, the first sub-group of the Society. His view of the strategic value in Professor Freddie encouraging like-minded biochemists to interact has done much to Gutfreund during his provide the critical mass necessary for sustaining excellence in the presentation ‘Development various sub-disciplines of biochemistry. of kinetics in biology’.

The talks reflected Professor about how proteins function. and his family. The dinner was Gutfreund’s many contributions In particular, he has made major followed by entertaining and to the study of biochemistry and contributions to the development affectionate talks presented biophysics. His early prominence of transient and relaxation kinetic by Nigel Scrutton, the present arose from developing the method- methods including stopped-flow, Chairman of the Molecular Speakers and Chairmen: ology to study fast events on quenched-flow and pressure- Enzymology Group, Hugh Back row (from left to enzymes which are now central to jump techniques. He has written Huxley, a long-time friend right): R.S. Goody, the field of molecular enzymology. influential books on enzymology from the Cambridge days back H.E. Huxley, K.C. Holmes, After beginning in physical and thermodynamics culminating in the 1950s, and Kenneth Holmes, D.R. Trentham, B.D. Sykes, biochemistry, he moved on to in his most recent book Kinetics a Director of the Max Planck S.E. Halford. Front row detailed studies of chemical for the Life Sciences. This seminal Institute in Heidelberg where (from left to right): mechanism of enzyme catalysis work brought together common Freddie has been a frequent J.F. Eccleston, M.A. Geeves, and, in particular, showed the conceptual approaches to the study Visiting Scientist over the T.J.T. Pinheiro, importance of ligand-induced of dynamic phenomena from the past decade. H. Gutfreund, J. Howard. changes in protein conformation level of purified individual proteins for defining the biological function to whole cells, organisms and of proteins. In hindsight, this populations. As such, it forms a appears like a natural progression fitting climax to a career that from physico-chemical mechanisms began on the firm foundation to ligand-induced conformational of physico-chemical studies of changes to the role of proteins in proteins and gradually embraced mediating the response of an more and more of the biological organism to its environment. processes that proteins direct. A central theme of Professor The meeting was followed by Gutfreund’s work and writing a reception and dinner to which has been the importance of new we were delighted to welcome technology in developing ideas Freddie Gutfreund’s wife Mary,