Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI020770-12
Application #
2061324
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1984-12-01
Project End
1998-06-30
Budget Start
1996-07-01
Budget End
1997-06-30
Support Year
12
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of Pennsylvania
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
042250712
City
Philadelphia
State
PA
Country
United States
Zip Code
19104
Kim, Y; Valentine, K; Opella, S J et al. (1998) Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers. Protein Sci 7:342-8
Marassi, F M; Ramamoorthy, A; Opella, S J (1997) Complete resolution of the solid-state NMR spectrum of a uniformly 15N-labeled membrane protein in phospholipid bilayers. Proc Natl Acad Sci U S A 94:8551-6
Almeida, F C; Opella, S J (1997) fd coat protein structure in membrane environments: structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix. J Mol Biol 270:481-95
Gesell, J; Zasloff, M; Opella, S J (1997) Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution. J Biomol NMR 9:127-35
Almeida, F C; Opella, S J (1997) Measurement of 1H T1 rho in a uniformly 15N-labeled protein in solution with heteronuclear two-dimensional spectroscopy. J Magn Reson 124:509-11
Klassen, R B; Opella, S J (1997) NMR studies of peptides and proteins associated with membranes. Methods Mol Biol 60:271-97
Howard, K P; Opella, S J (1996) High-resolution solid-state NMR spectra of integral membrane proteins reconstituted into magnetically oriented phospholipid bilayers. J Magn Reson B 112:91-4
Bechinger, B; Gierasch, L M; Montal, M et al. (1996) Orientations of helical peptides in membrane bilayers by solid state NMR spectroscopy. Solid State Nucl Magn Reson 7:185-91
Tobias, D J; Gesell, J; Klein, M L et al. (1995) A simple protocol for identification of helical and mobile residues in membrane proteins. J Mol Biol 253:391-5
Opella, S J; Kim, Y; McDonnell, P (1994) Experimental nuclear magnetic resonance studies of membrane proteins. Methods Enzymol 239:536-60

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