HRMAS NMR observation of β-sheet secondary structure on a water swollen solid support

Journal of Peptide Science

Volumn 9, Issue 1, 2003, Pages 47-53

  Rousselot Pailley, Pierre ^a   Boutillon, Christophe ^a   Wieruszeski, Jean Michel ^a   Lippens, Guy ^a  

^a INSTITUT DE BIOLOGIE DE LILLE   (France)

Author keywords

HRMAS NMR; Intramolecular sheet; Peptide; Secondary structure; Solid phase peptide synthesis

Indexed keywords

ALANINE; ASPARAGINE; ASPARTIC ACID; GLUTAMINE; GLYCINE; PEPTIDE; PROLINE; RESIN; SERINE; TYROSINE; WATER;

AQUEOUS SOLUTION; BETA SHEET; CHEMICAL PARAMETERS; CONTROLLED STUDY; NUCLEAR MAGNETIC RESONANCE; PH; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; REVIEW; SOLID;

MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; WATER;

EID: 0037261980     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/psc.431     Document Type: Review

References (26)

1. Muñoz V, Serrano L. Elucidating the folding problem of helical peptides in aqueous solution using empirical parameters. Nature Struct. Biol. 1994; 1: 399-409.
2. Muñoz V, Serrano L. Elucidating the folding problem of helical peptides II. Helix macrodipole effects and rational modification of the helical content of peptides. J. Mol. Biol. 1994; 245: 275-296.
3. Koo EH, Lansbury PT Jr, Kelly JW. Amyloid diseases: Abnormal protein aggregation in neurodegeneration. Proc. Natl Acad. Sci. 1999; 96: 9989-9990.
4. Hendrick RW, Hartl FU. Molecular chaperone functions of heat shock proteins. Ann. Rev. Biochemistry 1993; 62: 349-384.
5. Buchner J, Schmidt M, Fuchs M, Jaenicke R, Rudolph R, Schmid FX, Kiefhaber T. GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry 1991; 30: 1586-1591.
6. Stempfer G, Höll-Neugebauer B, Rudolph R. Improved refolding of an immobilized fusion protein. Nature Biotech. 1996; 14: 329-334.
7. Warras R, Wieruszeski JM, Boutillon C, Lippens G. High-Resolution Magic Angle Spinning NMR Study of Resin-Bound Polyalanine Peptides. J. Am. Chem. Soc. 2000; 122: 1789-1795.
8. 1H NMR in solid-phase organic synthesis. J. Org. Chem. 1994; 59: 7955-7956.
9. Anderson RC, Stokes JP, Shapiro MJ. Tetrahedron Lett. Structure determination in combinatorial chemistry: Utilization of magic angle spinning HMQC and TOCSY NMR spectra in the structure determination of Wang-bound lysine. 1995; 36: 5311-5314.
10. Furrer J, Piotto M, Bourdonneau M, Limal D, Guichard G, Elbayed K, Raya J, Briand JP, Bianco A. Evidence of secondary structure by high-resolution magic angle spinning NMR spectroscopy of a bioactive peptide bound to different solid supports. J. Am. Chem. Soc. 2001; 123: 4130-4138.
11. Ashish A, Wimley WC. Visual detection of specific, native interactions between soluble and microbead-tethered alpha-helices from membrane proteins. Biochemistry 2001; 40: 13753-13759.
12. Santini R, Griffith MC, Qi M. Tetrahedron Lett. A Measure of Solvent Effects on Swelling of Resins for Solid Phase Organic Synthesis. 1998; 39: 8951-8954.
13. Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wütrich K. Recommendations for the Presentation of NMR Structures of Proteins and Nucleic Acids. J. Biomol. NMR 1998; 12: 1-23.
14. Lippens G, Dhalluin C, Wieruszeski JM. An Improved Homonuclear TOCSY Experiment with Minimal Water Saturation. J. Biomol. NMR 1995; 5: 327-331.
15. Nirmala NR, Wagner G. Measurement of 13C relaxation times in protein by two-dimensional heteronuclear 1H-13C correlation spectroscopy. J. Am. Chem. Soc. 1988; 110: 7557-7558.
16. Blanco FJ, Angeles Jiménez M, Herranz J, Rico M, Santoro J, Nieto JL. NMR evidence of a short linear peptide that folds into a β-hairpin in aqueous solution. J. Am. Chem. Soc. 1993; 115: 5887-5888.
17. Meldal M. PAGA: A flow stable polyethylene glycol dimethyl acrylamide copolymer for solid phase synthesis. Tetrahedron Lett. 1992; 33: 3077-3080.
18. Atherton E, Clive DL, Sheppard RC. Polyamide Supports for Polypeptide Synthesis. J. Am. Chem. Soc. 1975; 97: 6584-6585.
19. Renil M, Meldal M. POEPOP and POEPS: Inert Polyethylene Glycol Crosslinked Polymeric Supports for Solid Synthesis. Tetrahedron Lett. 1996; 37: 6185-6188.
20. Wishart DS, Sykes BD. Identification of Protein Secondary Structure Using 13C Chemical-Shift Data. J. Biomol. NMR 1994; 4: 171-180.
21. Wishart DS, Bigam CG, Holm A, Hodges RS, Sykes BD. 1H, 13C and 15N Random Coil Chemical Shifts of the Common Amino Acids: L Investigations of Nearest Neighbor Effects. J. Biomol. NMR 1995; 5: 67-81.
22. Wütrich K. NMR of Protein and Nucleic Acids. Wiley & Sons: New York, 1986.
23. Grotli M, Gotfredsen CH, Rademann J, Buchardt J, Clark AJ, Duus JO, Meldal M. Physical properties of poly(ethylene glycol) (PEG)-based resins for combinatorial solid phase organic chemistry: A comparison of PEG-cross-linked and PEG-grafted resins. J. Comb. Chem. 2000; 2: 108-119.
24. Bianco A, Furrer J, Limal D, Guichard G, Piotto M, Raya J, Elbayed K, Briand JP. Multi-step synthesis of 2,5-diketopiperazines on different solid supports monitored by high resolution magic angle spinning NMR spectroscopy. J. Comb. Chem. 2000; 6: 681-690.
25. Dhalluin C, Boutillon C, Tartar A, Lippens G. Magic Angle Spinning Nuclear Magnetic Resonance in Solid-Phase Peptide Synthesis. J. Am. Chem. Soc. 1997: 119: 10494-10500.
26. ur sequence was submitted to the following web site in order to compute the pI: of the peptide http://www.embl-heidelberg.de/cgi/pi-wrapper.plO