Long-range 1H-19F distance measurement in peptides by solid-state NMR

Sungsool Wi; Neeraj Sinha; Mei Hong

doi:10.1021/ja0462732

Long-range 1H-19F distance measurement in peptides by solid-state NMR

J Am Chem Soc. 2004 Oct 13;126(40):12754-5. doi: 10.1021/ja0462732.

Authors

Sungsool Wi¹, Neeraj Sinha, Mei Hong

Affiliation

¹ Department of Chemistry, Iowa State University, Gilman 0108, Ames, IA 50011, USA.

PMID: 15469252
DOI: 10.1021/ja0462732

Abstract

A new NMR technique for determining long-range 1H-19F distances in solids is demonstrated. Using a modified rotational-echo double resonance (REDOR) sequence involving 1H homonuclear decoupling and composite 19F pulses, we show that it is possible to determine 1H-19F distances to approximately 8 A. The detrimental effect of the large 19F chemical shift to REDOR dephasing is partially compensated for by the composite pulse, 90 degrees 225 degrees 315 degrees . The 1HNLeu-19FPhe distance in the peptide f-MLF-OH was found to be 7.7 A. This was used to refine the Phe side chain conformation. The 1H-19F REDOR technique should be useful for restraining the three-dimensional structure of proteins.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Anisotropy
Chemotactic Factors / chemistry
Dipeptides / chemistry*
Fluorine
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular / methods*
Peptides / chemistry*
Protons

Substances

Chemotactic Factors
Dipeptides
Peptides
Protons
N-formylmethionylphenylalanine
Fluorine