Abstract

Solid state NMR spectroscopy will be used to study polycrystalline and amorphous peptides. The conformation and dynamics of peptides specifically synthesized to have well defined structural features in the solid state will be described. This new research on peptides in the solid state will be complementary to on going research on these same peptides in solution and allow important questions about the differences in conformation in solutions and in crystals to be answered. Several of the NMR experiments give unique information; in particular the details of bond geometries from 13C-14N dipolar couplings and 13C isotropic chemical shifts, the existence of asymmetric or multiple conformations from 13C chemical shifts and the dynamics of aromatic rings from the averaging of 2H quadrupole and 13C chemical shift powder patterns. The use of these peptides as model compounds for biological solid state NMR will lead to further development of the techniques and instrumentation.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM029754-05
Application #
3277398
Study Section
(SSS)
Project Start
1982-01-01
Project End
1987-12-31
Budget Start
1986-01-01
Budget End
1986-12-31
Support Year
5
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
University of Pennsylvania
Department
Type
Schools of Arts and Sciences
DUNS #
042250712
City
Philadelphia
State
PA
Country
United States
Zip Code
19104

  Publications

Park, Sang Ho; Das, Bibhuti B; De Angelis, Anna A et al. (2010) Mechanically, magnetically, and ""rotationally aligned"" membrane proteins in phospholipid bilayers give equivalent angular constraints for NMR structure determination. J Phys Chem B 114:13995-4003
Nevzorov, Alexander A; Mesleh, Michael F; Opella, Stanley J (2004) Structure determination of aligned samples of membrane proteins by NMR spectroscopy. Magn Reson Chem 42:162-71
Zeri, Ana Carolina; Mesleh, Michael F; Nevzorov, Alexander A et al. (2003) Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy. Proc Natl Acad Sci U S A 100:6458-63
Lee, Sangwon; Mesleh, Michael F; Opella, Stanley J (2003) Structure and dynamics of a membrane protein in micelles from three solution NMR experiments. J Biomol NMR 26:327-34
Mesleh, Michael F; Opella, Stanley J (2003) Dipolar Waves as NMR maps of helices in proteins. J Magn Reson 163:288-99
Marassi, Francesca M; Opella, Stanley J (2003) Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints. Protein Sci 12:403-11
Opella, Stanley J (2003) Membrane protein NMR studies. Methods Mol Biol 227:307-20
Nevzorov, Alexander A; Opella, Stanley J (2003) Structural fitting of PISEMA spectra of aligned proteins. J Magn Reson 160:33-9
Mesleh, M F; Valentine, K G; Opella, S J et al. (2003) Myristoylation as a general method for immobilization and alignment of soluble proteins for solid-state NMR structural studies. J Biomol NMR 25:55-61
Nevzorov, Alexander A; Opella, Stanley J (2003) A ""magic sandwich"" pulse sequence with reduced offset dependence for high-resolution separated local field spectroscopy. J Magn Reson 164:182-6

Showing the most recent 10 out of 53 publications