Resonance assignment strategies for the analysis of NMR spectra of proteins. Academic Article

abstract

• Determination of the high resolution solution structure of a protein using nuclear magnetic resonance (NMR) spectroscopy requires that resonances observed in the NMR spectra be unequivocally assigned to individual nuclei of the protein. With the advent of modern, two-dimensional NMR techniques arose methodologies for assigning the 1H resonances based on 2D, homonuclear 1H NMR experiments. These include the sequential assignment strategy and the main chain directed strategy. These basic strategies have been extended to include newer 3D homonuclear experiments and 2D and 3D heteronuclear resolved and edited methods. Most recently a novel, conceptually new approach to the problem has been introduced that relies on heteronuclear, multidimensional so-called triple resonance experiments for both backbone and sidechain resonance assignments in proteins. This article reviews the evolution of strategies for the assignment of resonances of proteins.

authors

• Wand, Joshua

published proceedings

• Mol Biotechnol

author list (cited authors)

• Leopold, M. F., Urbauer, J. L., & Wand, A. J.

citation count

• 22

complete list of authors

• Leopold, MF||Urbauer, JL||Wand, AJ

publication date

• August 1994

publisher

• Springer Nature  Publisher

published in

• Molecular Biotechnology  Journal

keywords

• Hydrogen
• Magnetic Resonance Spectroscopy
• Protein Conformation
• Proteins
• Solvents

Digital Object Identifier (DOI)

• 10.1007/BF02789290

start page

• 61

end page

• 93

volume

• 2

issue

• 1

URL

• http://dx.doi.org/10.1007/bf02789290