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Biochemistry
R. Bentley
J. Brodsky
J. Franzen
P. Grabowski
J. Hempel
L. Jen-Jacobson
K. Kiselyov
C. Peebles
J. Rosenberg
A. Schwacha
Cell Biology
J. Brodsky
A. Chung
J. Hildebrand
L. Jacobson
N. Kaufmann
K. Kiselyov
J. Pipas
M.-T. Sáens-Robles
W. Saunders
C. Walsh
Computational Biology
M. Grabe
J. Lawrence
J. Rosenberg
Developmental Biology
G. Campbell
D. Chapman
J. Hildebrand
B. Roman
S. Shostak
B. Stronach
V. Twombly
Ecology
T.-L. Ashman
W. Carson
W. Coffman
S. Kalisz
T. Katzner
R. Relyea
S. Tonsor
B. Traw
Evolution
T.-L. Ashman
A. Bledsoe
S. Kalisz
J. Lawrence
Z.-X. Luo
R. Relyea
S. Shostak
S. Tonsor
B. Traw
Genetics
K. Arndt
T.-L. Ashman
G. Campbell
D. Chapman
G. Hatfull
J. Hildebrand
L. Jacobson
S. Kalisz
J. Martens
W. Saunders
B. Stronach
S. Tonsor
R. Wood
Microbiology
J. Boyle
G. Hatfull
R. Hendrix
J. Lawrence
J. Pipas
M. Popa
I. Campbell
R.L. Duda
S. Godfrey
V. Oke
Molecular Biology
K. Arndt
J. Boyle
J. Franzen
P. Grabowski
G. Hatfull
R. Hendrix
L. Jen-Jacobson
J. Martens
C. Peebles
J. Pipas
J. Rosenberg
A. Schwacha
C. Walsh
Plant Biology
T.-L. Ashman
W. Carson
S. Kalisz
V. Oke
C. Partanen
S. Tonsor
B. Traw
Science Education
A. Bledsoe
K. Curto
S. Donovan
L. Daniels
S. Godfrey
N. Kaufmann
C. LaFave
J. Newman
V. Oke
E. Polinko
M. Popa
L. Roberts
T. Seiflein
R. Sherwin
A. Slinskey Legg
Structural Biology
M. Grabe
J. Hempel
R. Hendrix
L. Jen-Jacobson
J. Rosenberg
A. VanDemark
Former Faculty
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The incredible diversity of life on this planet is made possible by
proteins, all of which may be represented as linear heteropolymers of the
same 20 amino acids, acting in specific catalytic and/or structural roles.
The number of possible linear combinations of these amino acids in the
average-sized protein chain exceeds the extimated number of atoms in the
universe, and is thus fully compatible with the diversity of life. In the
extreme, examples abound of single amino acid changes in a single protein
in an organism which carry fatal consequences. Members of the Structural Biology
Group in the Deaprtment of Biological Sciences,
each working in their own system, seek to understand the details of both
normal and mutant protein interactions, through a combination of techniques
including X-ray crystallography, kinetic analysis, site-directed
mutagenesis, and chemical sequence analysis.
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