Neutron scattering techniques will be applied to the elucidation of a variety of structural problems in biology. Distance methods will be used to complete the low resolution map of the 30S ribosomal subunit of E. coli which is already two thirds done. The map will be extended to include the binding sites of factors and tRNA. Individual ribosomal proteins will be isolated from overproducing strains of E. coli. These materials will be studied by a variety of techniques including neutron scattering in order to discover what the true native configuration is of these molecules. Promising preliminary results have been obtained by inelastic neutron scattering. This new method may be useful in studies of the dynamics of protein molecules. Several systems in which structural changes are known to occur will be studied by this technique to see what the dynamic correlates are (e.g. ribosomal RNA during ribosome assembly). Finally, neutron methods will be used to study the interaction of proteins and peptides with lipid bilayers in order to test ideas of membrane protein insertion and folding.

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI020466-03
Application #
3130166
Study Section
Biophysics and Biophysical Chemistry A Study Section (BBCA)
Project Start
1983-08-01
Project End
1986-11-30
Budget Start
1985-08-01
Budget End
1986-11-30
Support Year
3
Fiscal Year
1985
Total Cost
Indirect Cost
Name
Yale University
Department
Type
Schools of Arts and Sciences
DUNS #
082359691
City
New Haven
State
CT
Country
United States
Zip Code
Capel, M S; Ramakrishnan, V (1988) Neutron-scattering topography of proteins of the small ribosomal subunit. Methods Enzymol 164:117-31
Capel, M S; Kjeldgaard, M; Engelman, D M et al. (1988) Positions of S2, S13, S16, S17, S19 and S21 in the 30 S ribosomal subunit of Escherichia coli. J Mol Biol 200:65-87
Capel, M S; Engelman, D M; Freeborn, B R et al. (1987) A complete mapping of the proteins in the small ribosomal subunit of Escherichia coli. Science 238:1403-6
Popot, J L; Gerchman, S E; Engelman, D M (1987) Refolding of bacteriorhodopsin in lipid bilayers. A thermodynamically controlled two-stage process. J Mol Biol 198:655-76
Trewhella, J; Popot, J L; Zaccai, G et al. (1986) Localization of two chymotryptic fragments in the structure of renatured bacteriorhodopsin by neutron diffraction. EMBO J 5:3045-9
Popot, J L; Trewhella, J; Engelman, D M (1986) Reformation of crystalline purple membrane from purified bacteriorhodopsin fragments. EMBO J 5:3039-44
Dumont, M E; Trewhella, J; Engelman, D M et al. (1985) Stability of transmembrane regions in bacteriorhodopsin studied by progressive proteolysis. J Membr Biol 88:233-47