Abstract

Experiments are proposed to study ligand diffusion in proteins. We will extend studies of xenon, myoglobin using new ligands. Work on a novel nanosecond circular dichroism instrument will proceed. It will be used to examine carbon monoxide photolysis in myoglobin and hemoglobin. We also suggest studies of protein folding based on the use of spin labels to learn about the structure of kinetic intermediates and the use of specific amino acid substitutions to study kinetic mechanisms. Finally, a set of experiments is devoted to the way solvent alters protein and peptide conformation.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
2R01GM019267-15
Application #
3269583
Study Section
Biophysics and Biophysical Chemistry A Study Section (BBCA)
Project Start
1977-12-01
Project End
1991-01-31
Budget Start
1986-02-01
Budget End
1987-01-31
Support Year
15
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
University of California San Francisco
Department
Type
Schools of Pharmacy
DUNS #
073133571
City
San Francisco
State
CA
Country
United States
Zip Code
94143

  Publications

Guiles, R D; Basus, V J; Sarma, S et al. (1993) Novel heteronuclear methods of assignment transfer from a diamagnetic to a paramagnetic protein: application to rat cytochrome b5. Biochemistry 32:8329-40
Kosen, P A; Marks, C B; Falick, A M et al. (1992) Disulfide bond-coupled folding of bovine pancreatic trypsin inhibitor derivatives missing one or two disulfide bonds. Biochemistry 31:5705-17
Guiles, R D; Basus, V J; Kuntz, I D et al. (1992) Sequence-specific 1H and 15N resonance assignments for both equilibrium forms of the soluble heme binding domain of rat ferrocytochrome b5. Biochemistry 31:11365-75
Hurle, M R; Eads, C D; Pearlman, D A et al. (1992) Comparison of solution structures of mutant bovine pancreatic trypsin inhibitor proteins using two-dimensional nuclear magnetic resonance. Protein Sci 1:91-106
Hurle, M R; Anderson, S; Kuntz, I D (1991) Confirmation of the predicted source of a slow folding reaction: proline 8 of bovine pancreatic trypsin inhibitor. Protein Eng 4:451-5
Altman, J D; Henner, D; Nilsson, B et al. (1991) Intracellular expression of BPTI fusion proteins and single column cleavage/affinity purification by chymotrypsin. Protein Eng 4:593-600
Bradley, E K; Thomason, J F; Cohen, F E et al. (1990) Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance. J Mol Biol 215:607-22
Guiles, R D; Altman, J; Kuntz, I D et al. (1990) Structural studies of cytochrome b5: complete sequence-specific resonance assignments for the trypsin-solubilized microsomal ferrocytochrome b5 obtained from pig and calf. Biochemistry 29:1276-89
Hurle, M R; Marks, C B; Kosen, P A et al. (1990) Denaturant-dependent folding of bovine pancreatic trypsin inhibitor mutants with two intact disulfide bonds. Biochemistry 29:4410-9
Babbitt, P C; West, B L; Buechter, D D et al. (1990) Removal of a proteolytic activity associated with aggregates formed from expression of creatine kinase in Escherichia coli leads to improved recovery of active enzyme. Biotechnology (N Y) 8:945-9

Showing the most recent 10 out of 18 publications