| People
- Faculty
- Professor:
Frederick Dahlquist |
| Field(s): |
Biochemistry |
 |
| Email: |
dahlquist@chem.ucsb.edu |
| Phone: |
(805)
893-5326 |
Fax:
(805)
893- |
| Office: |
1126C Chem |
 |
Selected
Publications |
 |
Go
to Research Group website (coming soon!) |
| Bio: |
B.A., Wabash College, 1964. Ph.D., California Institute
of Technology, 1969 (Michael Raftery). Postdoctoral: University
of California, Berkeley, 1969-71 (Daniel E. Koshland).
Honors and Awards: Miller Research Fellow, University
of California, Berkeley, 1969-71; Alfred P. Sloan Research
Fellow, 1975-77; Member, NSF Advisory Committee for Physiology,
Cellular, and Molecular Biology, 1980 present; Faculty
Research Award from the American Cancer Society, 1981-86;
Elected Fellow, American Academy of Microbiology, 1998;
Director, Institute of Molecular Biology, 119-98. |
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Research
Interests
Our research group is interested in the relationships between
protein structure and function. While the investigation of
this question is not restricted to any specific technique,
nuclear magnetic resonance offers a particularly useful and
powerful approach to the problem and is relied on heavily.
Several molecular systems are under investigation. For instance,
one problem is how the dynamics of a protein are related to
its structure and thermodynamic stability. Another concerns
how extra-cellular information is gathered and utilized by
protein complexes to generate signals that regulate biochemical
activity inside the cell.
One protein we often study is the lysozyme of bacteriophage
T4. Nuclear magnetic resonance (NMR) offers an unusually powerful
method to investigate the dynamics of this protein. NMR can
be exploited in a number of ways to monitor the structure
and dynamics of the protein. The laboratory is especially
interested in defining the folding pathway of the protein
in both an energetic and a kinetic sense.
The second major area of interest is the phenomenon of chemotaxis
in bacteria. When E. coli are placed in concentration gradients
of certain chemicals, they either accumulate at the high concentration
(for attractants) or low concentration (for repellents) regions
of the gradient. The bacteria sense temporal changes in the
concentration of attractant or repellent molecules and change
their swimming behavior accordingly. This process requires
sensing the concentrations of attractant or repellent, behavioral
response to rapid changes in these concentrations and relatively
slow adaptation to the new concentrations, which returns the
swimming behavior to the unstimulated condition. Adaptation
is associated with the reversible methylation of four transmembrane
receptors. These proteins receive environmental information
from outside the membrane and transmit that information to
the cytoplasm. The interests of the laboratory are in defining
how environmental information is transmitted across the inner
membrane and how that information is used to control the activity
of a specialized protein kinase (CheA) that interacts with
the receptors via an adapter protein (CheW). One (CheY) of
the two substrates of the kinase plays a central role in modulating
the sense of rotation of the flagellar rotary motors. We are
using NMR and other methods to understand the structures,
dynamics and interactions of the proteins involved in this
signaling system. Below is a model of the solution structure
of CheW.

Current
Research
Coming
soon!
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| Selected
Research Publications |
| Dyer, CM, Collin M. , Dahlquist, FW, et al. Switched or not?: the structure of unphosphorylated CheY bound to the N terminus of FliM J BACTERIOL 188 (21): 7354-7363 NOV 2006. |
| Hamel, D, Zhou, HJ, Dahlquist, FW Interaction of the phosphotransfer and catalytic domains of the histidine autokinase CheA. J GEN PHYSIOL 128 (1): - 4 JUL 2006. |
| Dahlquist, FW Slip sliding away: new insights into DNA-protein recognition NAT CHEM BIOL 2 (7): 353-354 JUL 2006. |
| Hamel, DJ, Dahlquist, FW The contact interface of a 120 kD CheA-CheW complex by methyl TROSY interaction spectroscopy J AM CHEM SOC 127 (27): 9676-9677 JUL 13 2005. |
| Korzhnev, DM, Orekhov, VY, Dahlquist, FW, et al. Off-resonance R-1 rho relaxation outside of the fast exchange limit: An experimental study of a cavity mutant of T4 lysozyme J BIOMOL NMR 26 (1): 39-48 MAY 2003. |
| Griswold, IJ, Dahlquist, FW The dynamic behavior of CheW from Thermotoga maritima in solution, as determined by nuclear magnetic resonance: implications for potential protein-protein interaction sites BIOPHYS CHEM 101: 359-373 DEC 10 2002. |
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