Abstract

This Program Project deals with protein structure, function, and engineering. Five members of the MIT tenured staff are principal investigators of the Program. Emphasis is placed upon the integration of molecular biology, mutagenesis, and recombinant DNA technology with the manipulation and determination of protein structure. Because many of the individual efforts include common technologies, a core facility will be established. This facility will serve the needs of and integrate the projects of all members of the Program. Specific areas of research include the design of antibody binding sites, the nature of antigenic sites on protein and nucleic acid surfaces, the capacity of protein structure for redesign of active sites, and the delineation of structural motifs in protein nucleic- acid interactions. These investigations can lead to a deeper understanding of protein design and of the capacity of proteins to be reengineered for specific applications in the health sciences.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Program Projects (P01)
Project #
5P01GM037641-04
Application #
3096261
Study Section
Special Emphasis Panel (SSS (E))
Project Start
1987-01-01
Project End
1991-12-31
Budget Start
1990-01-01
Budget End
1990-12-31
Support Year
4
Fiscal Year
1990
Total Cost
Indirect Cost

  Institution

Name
Massachusetts Institute of Technology
Department
Type
Schools of Arts and Sciences
DUNS #
City
Cambridge
State
MA
Country
United States
Zip Code
02139

  Publications

Martinis, S A; Schimmel, P (1992) Enzymatic aminoacylation of sequence-specific RNA minihelices and hybrid duplexes with methionine. Proc Natl Acad Sci U S A 89:65-9
Miller, W T; Schimmel, P (1992) A retroviral-like metal binding motif in an aminoacyl-tRNA synthetase is important for tRNA recognition. Proc Natl Acad Sci U S A 89:2032-5
Miller, W T; Hill, K A; Schimmel, P (1991) Evidence for a ""cysteine-histidine box"" metal-binding site in an Escherichia coli aminoacyl-tRNA synthetase. Biochemistry 30:6970-6
Kamradt, T; Soloway, P D; Perkins, D L et al. (1991) Pertussis toxin prevents the induction of peripheral T cell anergy and enhances the T cell response to an encephalitogenic peptide of myelin basic protein. J Immunol 147:3296-302
Musier-Forsyth, K; Usman, N; Scaringe, S et al. (1991) Specificity for aminoacylation of an RNA helix: an unpaired, exocyclic amino group in the minor groove. Science 253:784-6
Musier-Forsyth, K; Scaringe, S; Usman, N et al. (1991) Enzymatic aminoacylation of single-stranded RNA with an RNA cofactor. Proc Natl Acad Sci U S A 88:209-13
Toth, M J; Schimmel, P (1990) A mutation in the small (alpha) subunit of glycyl-tRNA synthetase affects amino acid activation and subunit association parameters. J Biol Chem 265:1005-9
Lai, M Z; Jang, Y J; Chen, L K et al. (1990) Restricted V-(D)-J junctional regions in the T cell response to lambda-repressor. Identification of residues critical for antigen recognition. J Immunol 144:4851-6
Park, S J; Miller, W T; Schimmel, P (1990) Synthetic peptide model of an essential region of an aminoacyl-tRNA synthetase. Biochemistry 29:9212-8
Toth, M J; Schimmel, P (1990) Deletions in the large (beta) subunit of a hetero-oligomeric aminoacyl-tRNA synthetase. J Biol Chem 265:1000-4

Showing the most recent 10 out of 17 publications