The Raymond and Beverly Sackler International Prize in Biophysics has been awarded to Professor Wolfgang Helfrich (left), Free University Berlin, Germany, and Professor Carlos Bustamante (right), University of California, Berkeley, USA. The prize awards dedication to science, originality, and excellence with $100,000, which is shared equally between the two winners. The prize was presented at a ceremony on December 12, 2012, as part of the Sackler Biophysics Symposium at Tel Aviv University, Israel.
Wolfgang Helfrich received the award for his contributions to the biophysics of lipid bilayers and biological membranes. Helfrich’s research involves the study of membrane physics, in particular vesicle shapes, membrane shape fluctuations, the effect of electric fields on vesicles, and the superstructure of phospholipid membranes.
Wolfgang Helfrich studied Physics at the Universities of Göttingen, Munich, and Tübingen, all Germany, from 1951 to 1958, and obtained his Ph.D. at the Technical University of Munich in 1961. He did postdoctoral work at the University of Munich, the National Research Council of Canada in Ottawa, and the RCA Laboratories at Princeton, USA. Helfrich gained his Habilitation in 1967 in Munich and returned to RCA Laboratories. In 1970, he joined Hoffmann-LaRoche Laboratories in Basel, Switzerland, and built the first twisted-nematic liquid-crystal electro-optical display with Martin Schadt.
In 1973, Helfrich accepted a professorship at the Free University Berlin, Germany, where he remained until his retirement in 1997.
Carlos Bustamante received the award for his work on single molecule biophysics. He develops and uses a range of single-molecule detection and manipulation techniques, such as optical tweezers, single-molecule fluorescence microscopy, and Scanning Force Microscopy (SFM), to understand the behavior of DNA-binding molecular motors, the mechanical unfolding of globular proteins and RNAs, and mechanisms of transcription control in prokaryotes.
Carlos Bustamante studied at the Universidad Peruana Cayetano Heredia and the Universidad Nacional Mayor de San Marcos, both Peru, before gaining his Ph.D. from the University of California, Berkeley, USA, in 1981. He joined the University of New Mexico, USA, in 1982 as Assistant Professor and was promoted to full professor there in 1989. From 1991–1998, Bustamante was Professor at the University of Oregon, USA. In 1998, he took up his current role of Professor of Molecular and Cell Biology and Physics at the Departments of Physics, Chemistry, BioPhysics, and Molecular Cell Biology, University of California, Berkeley. Since 2005, Bustamante has also been the Chair of the Department of Physics at the same university.
Selected publications of Wolfgang Helfrich:
- Effect of thermal undulations on the bending elasticity and spontaneous curvature of fluid membranes,
H. A. Pinnow, W. Helfrich,
Eur. Phys. J. E 2000, 3(2), 149–157.
DOI: 10.1007/s101890070028 - Effects of a cosurfactant on the stretching and bending elasticities of a surfactant monolayer,
M. M. Kozlov , W. Helfrich,
Langmuir 1992, 8(11), 2792–2797.
DOI: 10.1021/la00047a035 - Bending elasticity of electrically charged bilayers: coupled monolayers, neutral surfaces, and balancing stresses,
M. Winterhalter , W. Helfrich,
J. Phys. Chem. 1992, 96(1), 327–330.
DOI: 10.1021/j100180a060
Selected publications of Carlos Bustamante:
- Counting single photoactivatable fluorescent molecules by photoactivated localization microscopy (PALM),
SangHyuk Lee, Jae Yen Shin, Antony Lee, Carlos Bustamante,
Proc. Natl. Acad. Sci. 2012, 109, 17436–17441.
DOI: 10.1073/pnas.1215175109 - Ribosomal protein S1 unwinds double-stranded RNA in multiple steps,
Xiaohui Qu, Laura Lancaster, Harry F. Noller, Carlos Bustamante, Ignacio Tinoco Jr.,
Proc. Natl. Acad. Sci. 2012, 109, 14458–14463.
DOI: 10.1073/pnas.1208950109 - The ribosome uses two active mechanisms to unwind messenger RNA during translation,
Xiohui Qu, Jin-Der Wen, Laura Lancaster, Harry F. Noller, Carlos Bustamante, Ignacio Tinoco Jr.,
Nature 2011, 475, 118–121.
DOI: 10.1038/nature10126
