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Peptides and the development of double- and triple-resonance solid-state NMR of aligned samples*
N. Sinha C.V. Grant K.S. Rotondi L. Feduik-Rotondi L.M. Gierasch S.J. Opella
N. Sinha, C.V. Grant and S.J. Opella, Department of Chemistry and Biochemistry, 9500 Gilman Drive, University of California, San Diego, La Jolla, CA 92093-0307, USA
K.S. Rotondi, L. Feduik-Rotondi and L.M. Gierasch, Department of Biochemistry and Molecular Biology, 710 North Pleasant Street, University of Massachusetts, Amherst, MA, USA
Correspondence to S.J. Opella
Department of Chemistry and Biochemistry
University of California
San Diego
Natural Sciences Building, Room 3119
9500 Gilman Drive, MC 0307, La Jolla
CA 92093-0307, USA
Tel.: 858-822-4820
Fax: 858-822-4921
E-mail:
sopella@ucsd.edu

  *This paper is dedicated to Vic Hruby to honor his many years of editorial service to the peptide scientific community. His energy, enthusiasm and selfless commitment to the broad needs of science are truly appreciated.

Copyright 2005 Blackwell Munksgaard
KEYWORDS
nuclear magnetic resonance • polarization inversion spin exchange at the magic angle • single crystal • solid-state • triple-resonance

ABSTRACT

Abstract: Peptides have been instrumental in the development of solid-state nuclear magnetic resonance (NMR) spectroscopy, and their roles in the development of solid-state NMR of aligned samples is reviewed. In particular, the roles of synthetic peptides in the development of triple-resonance methods are described. Recent developments of pulse sequences and NMR probes for triple-resonance NMR of aligned samples are presented.


Dates:
Received 10 March 2005 Accepted 20 March 2005

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