Abstract

Solid-state NMR spectroscopy will continue to be developed and applied to the study of peptides. Solid-state NMR studies of crystalline peptides and of peptides complexed with lipids and proteins offer favorable opportunities for both the development of spectroscopic methods and the application of these methods to important biological problems. Many biological properties are expressed by peptides, however the primary high resolution methods of structure determination, x-ray diffraction and multidimensional solution NMR spectroscopy, have considerable difficulty in dealing with peptides because they are difficult to crystallize and because of their conformational flexibility. The planned spectroscopic developments involve a wide variety of multidimensional solid-state NMR experiments on polycrystalline and single crystal samples of peptides. The applications are to 20 - 25 residue amphipathic and hydrophobic peptides in lipid bilayers and to several peptides bound to proteins.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM029754-14
Application #
2175610
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1982-01-01
Project End
1996-12-31
Budget Start
1995-01-01
Budget End
1995-12-31
Support Year
14
Fiscal Year
1995
Total Cost
Indirect Cost

  Institution

Name
University of Pennsylvania
Department
Chemistry
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
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
Mesleh, Michael F; Lee, Sangwon; Veglia, Gianluigi et al. (2003) Dipolar waves map the structure and topology of helices in membrane proteins. J Am Chem Soc 125:8928-35
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

Showing the most recent 10 out of 53 publications