While immobilized animic textile dyes have been found useful for rapid efficient purification of a variety of proteins, we belive that the utility of these immobilized dyes could be markedly extended to more weakly bound proteins as well as to nucleic acids, subcellular assemblies, membranes and whole cells. Such extension of technology will require quantitative assessment of the contribution of matrices, bridging reagents, immobilized dye concentration, affinity constants and kinetic on/off rates, and pH temperature and solvent polarity. Such measurements will be made on model immobilized dyes as well as on chromatographic columns where feasible. Procedures will also be explored to covalently label protein ligand sites to provide a spectral marker for peptide fragmentation resolution and for kinetic studies of the regeneration of functional ligand binding sites from complementary peptide fragments or from denatured intact polypeptide chains.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM022109-11
Application #
3270935
Study Section
Biophysics and Biophysical Chemistry A Study Section (BBCA)
Project Start
1981-07-01
Project End
1987-03-31
Budget Start
1986-04-01
Budget End
1987-03-31
Support Year
11
Fiscal Year
1986
Total Cost
Indirect Cost
Name
University of Iowa
Department
Type
Schools of Medicine
DUNS #
041294109
City
Iowa City
State
IA
Country
United States
Zip Code
52242
Park, S H; Shalongo, W; Stellwagen, E (1997) The role of PII conformations in the calculation of peptide fractional helix content. Protein Sci 6:1694-700
Park, S H; Shalongo, W; Stellwagen, E (1993) Residue helix parameters obtained from dichroic analysis of peptides of defined sequence. Biochemistry 32:7048-53
Kopperschlager, G; Bar, J; Stellwagen, E (1993) Limited proteolysis of yeast phosphofructokinase. Sequence locations of cleavage sites created by the actions of different proteinases. Eur J Biochem 217:527-33
Shalongo, W; Heid, P; Stellwagen, E (1993) Kinetic analysis of the hydrodynamic transition accompanying protein folding using size exclusion chromatography. 1. Denaturant dependent baseline changes. Biopolymers 33:127-34
Shalongo, W; Jagannadham, M; Stellwagen, E (1993) A reexamination of the conformational transitions of T4 thioredoxin. Biopolymers 33:903-13
Park, S H; Shalongo, W; Stellwagen, E (1993) Modulation of the helical stability of a model peptide by ionic residues. Biochemistry 32:12901-5
Shalongo, W; Jagannadham, M; Stellwagen, E (1993) Kinetic analysis of the hydrodynamic transition accompanying protein folding using size exclusion chromatography. 2. Comparison of spectral and chromatographic kinetic analyses. Biopolymers 33:135-45
Shalongo, W; Jagannadham, M V; Heid, P et al. (1992) A kinetic study of the folding of staphylococcal nuclease using size-exclusion chromatography. Biochemistry 31:11390-6
Shalongo, W; Jagannadham, M V; Flynn, C et al. (1989) Refolding of denatured ribonuclease observed by size exclusion chromatography. Biochemistry 28:4820-5
Kelley, R F; Shalongo, W; Jagannadham, M V et al. (1987) Equilibrium and kinetic measurements of the conformational transition of reduced thioredoxin. Biochemistry 26:1406-11

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