Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Program Projects (P01)
Project #
5P01GM038794-10
Application #
5212122
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
10
Fiscal Year
1996
Total Cost
Indirect Cost
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
Sanner, M F; Olson, A J (1997) Real time surface reconstruction for moving molecular fragments. Pac Symp Biocomput :385-96
Reva, B A; Finkelstein, A V; Sanner, M F et al. (1997) Residue-residue mean-force potentials for protein structure recognition. Protein Eng 10:865-76
Kriwacki, R W; Wu, J; Tennant, L et al. (1997) Probing protein structure using biochemical and biophysical methods. Proteolysis, matrix-assisted laser desorption/ionization mass spectrometry, high-performance liquid chromatography and size-exclusion chromatography of p21Waf1/Cip1/Sdi1. J Chromatogr A 777:23-30
Kolinski, A; Skolnick, J (1997) High coordination lattice models of protein structure, dynamics and thermodynamics. Acta Biochim Pol 44:389-422
Demchuk, E; Bashford, D; Case, D A (1997) Dynamics of a type VI reverse turn in a linear peptide in aqueous solution. Fold Des 2:35-46

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