Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Program Projects (P01)
Project #
3P01GM038794-03S1
Application #
3096279
Study Section
Special Emphasis Panel (SSS (D))
Project Start
1987-07-01
Project End
1992-06-30
Budget Start
1990-01-01
Budget End
1990-06-30
Support Year
3
Fiscal Year
1990
Total Cost
Indirect Cost
Name
Scripps Research Institute
Department
Type
DUNS #
City
San Diego
State
CA
Country
United States
Zip Code
92037
Karimi, A; Matsumura, M; Wright, P E et al. (1999) Characterization of monomeric and dimeric B domain of Staphylococcal protein A. J Pept Res 54:344-52
Larsen, T A; Olson, A J; Goodsell, D S (1998) Morphology of protein-protein interfaces. Structure 6:421-7
Olson, A J; Pique, M E (1998) Visualizing the future of molecular graphics. SAR QSAR Environ Res 8:233-47
Sikorski, A; Kolinski, A; Skolnick, J (1998) Computer simulations of de novo designed helical proteins. Biophys J 75:92-105
Dyson, H J; Bolinger, L; Feher, V A et al. (1998) Sequence requirements for stabilization of a peptide reverse turn in water solution--proline is not essential for stability. Eur J Biochem 255:462-71
Reymond, M T; Merutka, G; Dyson, H J et al. (1997) Folding propensities of peptide fragments of myoglobin. Protein Sci 6:706-16
Demchuk, E; Bashford, D; Gippert, G P et al. (1997) Thermodynamics of a reverse turn motif. Solvent effects and side-chain packing. J Mol Biol 270:305-17
Bai, Y; Karimi, A; Dyson, H J et al. (1997) Absence of a stable intermediate on the folding pathway of protein A. Protein Sci 6:1449-57
Reva, B A; Finkelstein, A V; Sanner, M et al. (1997) Recognition of protein structure on coarse lattices with residue-residue energy functions. Protein Eng 10:1123-30
Sanner, M F; Olson, A J (1997) Real time surface reconstruction for moving molecular fragments. Pac Symp Biocomput :385-96

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