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Society Fellows Named

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DMCG...@biophysics.faseb.org

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Sep 17, 1999, 3:00:00 AM9/17/99
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The Biophysical Society is proud to announce the Society Fellows for the
year 2000. This first class of Fellows consists of 39 distinguished
Society
members who have contributed to the highest level of the science of
biophysics.

Gary K. Ackers for his fundamental studies of biomolecule association and
cooperativity, particularly in hemoglobin, and for pioneering the
application of the methods and principles of equilibrium thermodynamics to
the study and dissection of function and organization in complex
macromolecular assemblies.

Richard W. Aldrich for his elegant and insightful work on gating of
sodium, potassium and calcium-activated potassium channels.

Clay M. Armstrong for the impact of his experimentation and original
thinking on the development of channel biophysics.

Daniel Axelrod for his pioneering research that helped develop the field
of
Total Internal Reflection Fluorescence (TIRF) microscopy. This work has
impacted biophysical research broadly from cell biology to single molecule
detection.

Robert L. Baldwin for his seminal contributions to the field of protein
folding.

Francisco Bezanilla for his work in channel biophysics that includes a
rare
combination of state-of-the-art techniques in molecular biology,
electrophysiology and spectroscopy.

Rodney L. Biltonen for his many original and significant contributions to
our understanding of fundamental biological thermodynamics and
of the kinetic basis of regulation of interacting biological systems.

Kevin P. Campbell for his research on the dystrophin-glycoprotein complex
of muscle and its role in normal skeletal muscle and in Duchenne muscular
dystrophy and his research in the field of voltage-dependent calcium
channels.

Charles R. Cantor for major contributions to the Genome project including
the development of methods for separating large DNA molecules,studies on
structural relationships in complex assemblies of proteins and nucleic
acids, and for sensitive detection of proteins and nucleic acids.

Donald L. D. Caspar for his pioneering research in structural biology
including determination of the first viral structures by x-ray
diffraction,and for his insightful work on viruses and structures of
crystals.

Carolyn Cohen for her structural studies of fibrous and contractile
proteins.

Donald M. Crothers for contributions to molecular biophysics and for his
pioneering contributions on the problems of RNA folding.

David Eisenberg for his unique contributions to the understanding of
protein structure and stability using x-ray crystallography and
computational modelling, and for relating structure to function by
biochemical and genetic methods.

S. Walter Englander for the development of models and methods that have
contributed to a much deeper understanding of the dynamic structural
processes of protein folding and hydrogen exchange rates.

Bertil Hille for his many seminal discoveries in the fields of ion
channels
and second messengers including studies on the mechanism of permeability
of
the acetylcholine receptor ion channel.

Barry Honig for his many seminal contributions in biophysics including
quantum chemistry, biophysics of color vision, protein folding,
electrostatics of proteins in DNA and protein structure prediction and
bioinformatics.
Wayne Hubbell for his development and application of site-directed spin
labeling.

Hugh E. Huxley for establishing the structural basis for muscle
contraction
using x-ray diffraction and electron microscopy.

William P. Jencks for his deep fundamental contributions to our
understanding of the basic chemistry underlying the mechanisms of enzyme
action.

Jack H. Kaplan for his highly significant contributions to the fields of
transport, membrane permeability and active transport and the introduction
of photorelease strategies.

Peter S. Kim for his outstanding contributions to our understanding of
fundamental aspects of protein folding and macromolecular recognition.

Susan Lowey for dissecting and characterizing the functional domains of
muscle myosins, including the effects of light chain phosphorylation on
the
structure and activity of smooth muscle myosin.

J. Andrew McCammon for his pioneering work in the development of
biomolecular dynamics, and computer models and simulation methods, and for
his work on motion in biomolecules, which provides a foundation for modern
theoretical understanding of protein dynamics.

Harden M. McConnell for fundamental contributions in molecular orbital
theory to explain electron distributions in aromatic radicals and in
kinetic
analysis of NMR spectra, for defining the range of motions possible for
membrane components, and for developing biological applications of spin
labeling.

Gerhard Meissner for his identification and characterization of the
ryanpodine receptors, which have been instrumental in opening a new era in
excitation-coupling studies and for seminal contributions to the field of
intracellular calcium signaling.

Peter B. Moore for pioneering the development of novel biophysical
approaches for obtaining structural information on macromolecular
assemblies.

V. Adrian Parsegian for his fundamental contributions to intermolecular
forces in biological systems through measuring, formulating, computing
and,
gauging the consequences of forces that organize biomolecules.

Thomas D. Pollard for major contributions in his research of the
biophysics and cell biology of the cytoskeleton.

Frederic M. Richards for seminal contributions to methods of protein
structure determination, for a long history of contributions to protein
structures, and for deep insights into the forces of organization,
packing,
and geometries in proteins.

Michael G. Rossmann for his fundamental contributions towards the
determination of the 3-D structure of viruses accomplished over many years
by his methodical and creative development of mathematical procedures,
unique biochemical and crystallographic techniques, and for identifying
the
Rossman fold.

Harold A. Scheraga for his pioneering development of theory and
experiments
that have led to a deeper understanding of protein structure and
properties.

Andrew P. Somlyo for his seminal contributions in collaboration with Avril
V. Somlyo to the understanding of the mechanism of contraction and its
regulation in smooth muscle as well as of excitation-coupling in skeletal
muscle.

Avril V. Somlyo for her seminal contributions in collaboration with Andrew
P. Somlyo to the understanding of the mechanism of contraction and its
regulation in smooth muscle as well as of excitation-coupling in skeletal
muscle.

Robert M. Stroud for his leadership for many years in shaping the field
of
x-ray structural studies of structure-function relationships in
macromolecules and for his mentoring an extraordinarily successful group
of
graduate students and postdoctoral fellows.

Andrew G. Szent-Gyorgyi for pivotal discoveries in the field of
contractile
protein biophysics including the demonstration that myosin can be
proteolytically cleaved into distinct domains, for the discovery of
myosin-dependent regulation of muscle contraction, and for the definition
of
a critical regulatory fragment of the scallop myosin.

Thomas E. Thompson for his many lasting contributions to research on
bilayer membranes and his impact throughout the field of membrane
biophysics.

Richard W. Tsien For his major contributions to understanding both the
fundamental biophysical and molecular properties of calcium channels, as
well as the clarification of the physiological function of the calcium
fluxes produced by these channels in important cellular and organismic
processes.

Watt W. Webb for his work in physical measurements that illuminate
cellular
events including an exhaustive and instructive set of FRAP measurements on
lateral movement in cells and in artificial lipid preparations and for a
breathtaking set of studies on live cells.

Annemarie Weber for her fundamental contributions towards understanding
the
regulation of muscle contraction and the dynamics of actin polymerization.


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