Alexander Hollaender Award in Biophysics

Alexander Hollaender Award in Biophysics

About the Alexander Hollaender Award in Biophysics

The Alexander Hollaender Award in Biophysics is presented every three years and carries with it a $20,000 prize. The Award recognizes outstanding contributions made to the field of biophysics. Henrietta W. Hollaender established the Alexander Hollaender Award in Biophysics in honor of her husband, Alexander W. Hollaender, whom brought to prominence the field of photobiology.  With an interest in the lethal and mutagenic effects of monochromatic ultra-violet radiation on cells, Dr. Hollaender identified the first clear indication that changes in nucleic acids needed to be analyzed, rather than proteins.    

Most Recent Recipient

Richard Henderson, member of the scientific staff in the MRC (Medical Research Council) Laboratory of Molecular Biology in Cambridge, U.K., received the 2016 Alexander Hollaender Award in Biophysics.

In 1975, Henderson and colleague Nigel Unwin determined the structure of bacteriorhodopsin—a light-driven proton pump found in the membrane of Archaea—using electron microscopy. This was revolutionary because the technique usually requires a stain that can obfuscate details, but Henderson and Unwin realized they could instead place the crystals on a thin carbon support and eliminate the stain. Starting in the 1990s, Henderson again revolutionized the field of structural biology when he turned his sights on another method for determining protein structure: cryoEM. In this technique, proteins are flash-frozen by plunging into liquid ethane then imaged with electron microscopy. Henderson and others made major improvements to the method—developing better sensors for electron microscopes, as well as better software for the system—that improved cryoEM to such an extent it is now the preferred technique for determining protein structures. Read more about Henderson's work»

Award History

The Alexander Hollaender Award in Biophysics was first awarded in 1998 to Wayne A. Hendrickson for his contributions to macromolecular crystallography, specifically his development of robust methods of phasing and refinement, and determination of complex and biologically important structures. Hendrickson is best known for his work pioneering multi-wavelength anomalous diffraction (MAD) and its use as an analytical tool for protein crystallography.  


Richard Henderson (2016)
For his pioneering work in the determination of atomic structure of a macromolecule by electron microscopy (EM). Henderson determined the first atomic structure of a 2-D protein crystalline array (bacteriorhodopsin) by EM. His identifications of the key bottlenecks for obtaining high-resolution EM structures has guided subsequent efforts to revolutionize single particle cryoEM for structural biology research at the atomic level.
Read more about Henderson's work

King-Wai Yau (2013)
For innovative, rigorous, and fundamental contributions to the biophysics of sensory transduction in rod, cone, and non-image visual systems and in olfaction.

Watt W. Webb (2010)
For pioneering the applications of rigorous physical principles to the development of optical tools that have broadly impacted our ability to examine biological systems.

Barry H. Honig (2007)
For pioneering theoretical and computational studies of electrostatic interactions in biological macromolecules and of the energetics of protein folding.

Carlos J. Bustamante (2004)
For his ingenious use of atomic force microscopy and laser tweezers to study the biophysical properties of proteins, DNA, and RNA, one molecule at a time.

David J. DeRosier (2001)
For his development of three-dimensional image reconstruction methods, which have revolutionized electron microscopy of subcellular structures and his analytical visualization of cellular motility mechanisms.

Wayne A. Hendrickson (1998)
For his contributions to macromolecular crystallography, in the development of robust methods of phasing and refinement, and in determination of complex and biologically important structures. 

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