Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM041905-08
Application #
2181117
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1989-07-01
Project End
1997-07-31
Budget Start
1996-08-01
Budget End
1997-07-31
Support Year
8
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Hebrew University of Jerusalem
Department
Type
DUNS #
600044978
City
Jerusalem
State
Country
Israel
Zip Code
91904
Schueler-Furman, O; Elber, R; Margalit, H (1998) Knowledge-based structure prediction of MHC class I bound peptides: a study of 23 complexes. Fold Des 3:549-64
Mohanty, D; Elber, R; Thirumalai, D et al. (1997) Kinetics of peptide folding: computer simulations of SYPFDV and peptide variants in water. J Mol Biol 272:423-42
Keasar, C; Elber, R; Skolnick, J (1997) Simultaneous and coupled energy optimization of homologous proteins: a new tool for structure prediction. Fold Des 2:247-59
Simmerling, C L; Elber, R (1995) Computer determination of peptide conformations in water: different roads to structure. Proc Natl Acad Sci U S A 92:3190-3
Carlson, M L; Regan, R; Elber, R et al. (1994) Nitric oxide recombination to double mutants of myoglobin: role of ligand diffusion in a fluctuating heme pocket. Biochemistry 33:10597-606
Chiancone, E; Elber, R; Royer Jr, W E et al. (1993) Ligand binding and conformation change in the dimeric hemoglobin of the clam Scapharca inaequivalvis. J Biol Chem 268:5711-8
Li, H; Elber, R; Straub, J E (1993) Molecular dynamics simulation of NO recombination to myoglobin mutants. J Biol Chem 268:17908-16
Gibson, Q H; Regan, R; Elber, R et al. (1992) Distal pocket residues affect picosecond ligand recombination in myoglobin. An experimental and molecular dynamics study of position 29 mutants. J Biol Chem 267:22022-34
Czerminski, R; Elber, R (1991) Computational studies of ligand diffusion in globins: I. Leghemoglobin. Proteins 10:70-80