Information about structures of biological molecules has often been used effectively to gain understanding of their functions. Biological function also involves dynamic processes, however, which are not amenable to study by many techniques used to determined equilibrium structural properties. Dynamics of biological systems are often studied by optical spectroscopy because optical spectra can be measured very rapidly. Absorption spectra are not sensitive to many structural changes, however, so it is often difficult to combine structural and dynamic information about biological processes. We have developed a technique which is very useful for linking this gap. This technique allows us to measure circular dichroism (CD) spectra, which are sensitive to structural properties of biomolecules, with nanosecond time resolution. The technique has been demonstrated effectively in a variety of nanosecond time scale studies. We now plan to extend the capabilities of the measurements to a broader spectral range and to better time resolution. We also plan to apply these measurements to the study of a variety of biologically interesting processes. These include ligand dissociation reactions in myoglobin and hemoglobin, studies of photolysis intermediates in bacteriorhodopsin, and studies of protein folding processes.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM035158-07
Application #
3287404
Study Section
Biophysical Chemistry Study Section (BBCB)
Project Start
1985-08-30
Project End
1993-07-31
Budget Start
1991-08-01
Budget End
1992-07-31
Support Year
7
Fiscal Year
1991
Total Cost
Indirect Cost
Name
University of California Santa Cruz
Department
Type
Schools of Arts and Sciences
DUNS #
City
Santa Cruz
State
CA
Country
United States
Zip Code
95064
Goldbeck, R A; Thomas, Y G; Chen, E et al. (1999) Multiple pathways on a protein-folding energy landscape: kinetic evidence. Proc Natl Acad Sci U S A 96:2782-7
Chen, E; Wood, M J; Fink, A L et al. (1998) Time-resolved circular dichroism studies of protein folding intermediates of cytochrome c. Biochemistry 37:5589-98
Chen, E; Lapko, V N; Song, P S et al. (1997) Dynamics of the N-terminal alpha-helix unfolding in the photoreversion reaction of phytochrome A. Biochemistry 36:4903-8
Goldbeck, R A; Sagle, L; Kim-Shapiro, D B et al. (1997) Evidence for heme-heme excitonic coupling in the Soret circular dichroism of hemoglobin. Biochem Biophys Res Commun 235:610-4
Chen, E; Goldbeck, R A; Kliger, D S (1997) Nanosecond time-resolved spectroscopy of biomolecular processes. Annu Rev Biophys Biomol Struct 26:327-55
Goldbeck, R A; Kim-Shapiro, D B; Kliger, D S (1997) Fast natural and magnetic circular dichroism spectroscopy. Annu Rev Phys Chem 48:453-79
Chen, E; Lapko, V N; Lewis, J W et al. (1996) Mechanism of native oat phytochrome photoreversion: a time-resolved absorption investigation. Biochemistry 35:843-50
Bjorling, S C; Goldbeck, R A; Paquette, S J et al. (1996) Allosteric intermediates in hemoglobin. 1. Nanosecond time-resolved circular dichroism spectroscopy. Biochemistry 35:8619-27
Goldbeck, R A; Paquette, S J; Bjorling, S C et al. (1996) Allosteric intermediates in hemoglobin. 2. Kinetic modeling of HbCO photolysis. Biochemistry 35:8628-39
Shapiro, D B; Esquerra, R M; Goldbeck, R A et al. (1996) A study of the mechanisms of slow religation to sickle cell hemoglobin polymers following laser photolysis. J Mol Biol 259:947-56

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